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Conserved domains on  [gi|161016828|ref|NP_031558|]
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branched-chain-amino-acid aminotransferase, cytosolic isoform 2 [Mus musculus]

Protein Classification

branched-chain amino acid aminotransferase family protein( domain architecture ID 1000621)

branched-chain amino acid aminotransferase family protein similar to branched-chain-amino-acid transaminase, which catalyzes the transamination of the branched-chain amino acids leucine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate

EC:  2.6.1.-
Gene Ontology:  GO:0004084|GO:0009081
SCOP:  4002874

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13357 super family cl36240
branched-chain amino acid aminotransferase; Provisional
33-386 1.48e-139

branched-chain amino acid aminotransferase; Provisional


The actual alignment was detected with superfamily member PRK13357:

Pssm-ID: 237363  Cd Length: 356  Bit Score: 401.45  E-value: 1.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  33 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 112
Cdd:PRK13357   8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 113 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 191
Cdd:PRK13357  87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 192 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 270
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 271 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 350
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 161016828 351 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 386
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
 
Name Accession Description Interval E-value
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
33-386 1.48e-139

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 401.45  E-value: 1.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  33 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 112
Cdd:PRK13357   8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 113 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 191
Cdd:PRK13357  87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 192 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 270
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 271 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 350
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 161016828 351 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 386
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
81-375 8.46e-130

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: 373.84  E-value: 8.46e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  81 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 160
Cdd:cd01557    2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 161 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 240
Cdd:cd01557   82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 241 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 320
Cdd:cd01557  160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161016828 321 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 375
Cdd:cd01557  233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
68-385 4.46e-104

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: 309.77  E-value: 4.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828   68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 147
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  148 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 226
Cdd:TIGR01123  81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  227 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  306 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 383
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311

                  ..
gi 161016828  384 EL 385
Cdd:TIGR01123 312 EV 313
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
68-378 3.89e-75

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: 234.70  E-value: 3.89e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 146
Cdd:COG0115    4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 147 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 225
Cdd:COG0115   79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:COG0115  150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016828 306 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 378
Cdd:COG0115  223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
94-343 3.63e-36

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


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 131.33  E-value: 3.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828   94 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 172
Cdd:pfam01063   2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  173 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 251
Cdd:pfam01063  70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  252 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 331
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
                         250
                  ....*....|..
gi 161016828  332 GTACVVCPVSDI 343
Cdd:pfam01063 210 NSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
33-386 1.48e-139

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 401.45  E-value: 1.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  33 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 112
Cdd:PRK13357   8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 113 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 191
Cdd:PRK13357  87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 192 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 270
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 271 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 350
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 161016828 351 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 386
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
81-375 8.46e-130

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: 373.84  E-value: 8.46e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  81 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 160
Cdd:cd01557    2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 161 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 240
Cdd:cd01557   82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 241 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 320
Cdd:cd01557  160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161016828 321 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 375
Cdd:cd01557  233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
68-385 4.46e-104

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: 309.77  E-value: 4.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828   68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 147
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  148 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 226
Cdd:TIGR01123  81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  227 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  306 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 383
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311

                  ..
gi 161016828  384 EL 385
Cdd:TIGR01123 312 EV 313
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
85-347 1.56e-76

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: 237.11  E-value: 1.56e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  85 ASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvpySTSASLYIR 163
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 164 PTFIGTEPSLGV--KKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGNYgASLLAQCEAVENG 241
Cdd:cd00449   69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGGE-KGVRLITSPDRRRAAPGGTGDAKTGGNL-NSVLAKQEAAEAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 242 CQQVLWLYGkDNQITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAle 321
Cdd:cd00449  147 ADEALLLDD-NGYVTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
                        250       260
                 ....*....|....*....|....*.
gi 161016828 322 gnrvKEMFGSGTACVVCPVSDILYKG 347
Cdd:cd00449  218 ----DEVFLTGTAAEVTPVTEIDGRG 239
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
68-378 3.89e-75

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: 234.70  E-value: 3.89e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 146
Cdd:COG0115    4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 147 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 225
Cdd:COG0115   79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:COG0115  150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161016828 306 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 378
Cdd:COG0115  223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
43-385 4.80e-67

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 217.79  E-value: 4.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02782  71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRN 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVkKPSKALLFVI-LSPVGPYFSSGsFTP 201
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGL-APAPEYTFLIyVSPVGNYFKEG-VAP 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 202 VSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKdnQITEVGTMNLFLYWINedgeeELAT 278
Cdd:PLN02782 229 INLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvHKK--YLEEVSSCNIFIVKDN-----VIST 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 279 PPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQmlHIPTMENG 358
Cdd:PLN02782 302 PAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGK--RVSYGEGG 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 161016828 359 PKLASRIL-GKLTDIQYGRVES--DWTIEL 385
Cdd:PLN02782 373 FGTVSQQLyTVLTSLQMGLIEDnmNWTVEL 402
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
45-385 7.66e-63

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 205.16  E-value: 7.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  45 DSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSA 124
Cdd:PLN03117  23 EELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 125 VRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSftPVSL 204
Cdd:PLN03117 103 DRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASS--GLNL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 205 WANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKDnqITEVGTMNLFLYWINedgeeELATPPL 281
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdaaTGKN--IEELSACNIFILKGN-----IVSTPPT 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGpkL 361
Cdd:PLN03117 254 SGTILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--L 324
                        330       340
                 ....*....|....*....|....*.
gi 161016828 362 ASRILGKLTDIQYGRVESD--WTIEL 385
Cdd:PLN03117 325 STKLHLILTNIQMGVVEDKkgWMVEI 350
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
43-380 5.14e-54

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 183.38  E-value: 5.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02259  57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGsFTPV 202
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 203 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYG-KDNQITEVGTMNLFLYwinedGEEELATPPL 281
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 361
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
                        330
                 ....*....|....*....
gi 161016828 362 ASRILGKLTDIQYGRVESD 380
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
43-385 9.98e-49

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 169.13  E-value: 9.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02883  53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPV 202
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 203 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLYWINedgeeELATPPL 281
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKnIEEVSAANIFLVKGN-----IIVTPAT 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 361
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
                        330       340
                 ....*....|....*....|....*.
gi 161016828 362 ASRILGKLTDIQYGRVE--SDWTIEL 385
Cdd:PLN02883 358 TQQLRSILLGIQTGSIQdtKDWVLQI 383
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
94-343 3.63e-36

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


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 131.33  E-value: 3.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828   94 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 172
Cdd:pfam01063   2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  173 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 251
Cdd:pfam01063  70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  252 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 331
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
                         250
                  ....*....|..
gi 161016828  332 GTACVVCPVSDI 343
Cdd:pfam01063 210 NSLRGVTPVSSI 221
PRK06606 PRK06606
branched-chain amino acid transaminase;
75-381 4.51e-30

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 117.17  E-value: 4.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  75 PFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIrLFRPDLNMDRMCRSA--VRTTLPmFDKEELLKCILQLLQIDQewv 152
Cdd:PRK06606  17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 153 pystSASLYIRP-TFIGTEpSLGVKKPS-KALLFVILSPVGPYFSSGSFTP-----VSLW--ANPKYI--RAwkggtgdc 221
Cdd:PRK06606  92 ----LKSAYIRPlVFVGDE-GLGVRPHGlPTDVAIAAWPWGAYLGEEALEKgirvkVSSWtrHAPNSIptRA-------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 222 KMGGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 301
Cdd:PRK06606 159 KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 302 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI-LYKgqmlhIPTMENGPkLASRILGKLTDIQYGRVE-- 378
Cdd:PRK06606 233 G-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREVdGRQ-----IGNGKRGP-ITEKLQSAYFDIVRGRTEky 299

                 ...
gi 161016828 379 SDW 381
Cdd:PRK06606 300 AHW 302
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
75-343 7.12e-26

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: 105.52  E-value: 7.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828   75 PFGNLPIHPAASVLHYAVELFEGLKAFRGvDNKIRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvp 153
Cdd:TIGR01122   8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  154 ySTSASLYIRP-TFIGTEpSLGVKKPSKAL--LFVILSPVGPY-----FSSGSFTPVSLW--ANPKYIrawkggTGDCKM 223
Cdd:TIGR01122  81 -NNLRSAYIRPlVFRGDG-DLGLNPRAGYKpdVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  224 GGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGe 303
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 161016828  304 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV 259
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
95-343 2.99e-21

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: 92.28  E-value: 2.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  95 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSASLYIRPTFiGTEP- 171
Cdd:cd01558   28 YEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIPY-TREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPr 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 172 SLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLwANPKYIRaWkggtGDCKM-GGNYGASLLAQCEAVENGCQQVlWLYG 250
Cdd:cd01558   96 GHDFPKCVKPTVVIITQPLPLPPAELLEKGVRV-ITVPDIR-W----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 251 KDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFG 330
Cdd:cd01558  169 ADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEERPFSLEELYTA------DEVFL 236
                        250
                 ....*....|...
gi 161016828 331 SGTACVVCPVSDI 343
Cdd:cd01558  237 TSTTAEVMPVVEI 249
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
95-343 2.64e-14

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 72.60  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  95 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSAslYIRPTFIGTEPS 172
Cdd:PRK08320  33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 173 LGV--KKPSKALLFVILSPVGPYFssGSF---------------TPVSLWANPKYIrawkggtgdckmggNYGASLLAQC 235
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYP--GELyekglkvitvstrrnRPDALSPQVKSL--------------NYLNNILAKI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 236 EAVENGCQQVLWLygkDNQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTM 313
Cdd:PRK08320 164 EANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTL 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 161016828 314 DDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK08320 235 HDLYTA------DEVFLTGTAAEVIPVVKV 258
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
88-321 1.87e-11

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: 63.48  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  88 LHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIdqewvpySTSASLYIRPTFI 167
Cdd:cd01559    4 FAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAA-------NDIDEGRIRLILS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 168 -GTEP----SLGVKKPSkALLFVILSPVGPYFSSGS--FTPVSLWANP-----KYIrawkggtgdckmggNYGASLLAQC 235
Cdd:cd01559   72 rGPGGrgyaPSVCPGPA-LYVSVIPLPPAWRQDGVRliTCPVRLGEQPllaglKHL--------------NYLENVLAKR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 236 EAVENGCQQVLWLYGKDNqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRQSILELAQQWGEFKVcERHLTMDD 315
Cdd:cd01559  137 EARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGYAVD-ERPLRLED 209

                 ....*.
gi 161016828 316 LATALE 321
Cdd:cd01559  210 LLAADE 215
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
77-343 9.68e-10

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 58.81  E-value: 9.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  77 GNLPIHPAASvlH---YAVELFEGLKAFRGVdnkirlfRPDLnmDRMC----RSAVRTTL-PMFDKEELLKCILQLLQid 148
Cdd:PRK13356  18 GNVPIMGPAD--HaawLGSTVFDGARAFEGV-------TPDL--DLHCarvnRSAEALGLkPTVSAEEIEALAREGLK-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 149 qewvPYSTSASLYIRPTFIGTEPSLGVKKPSK-----AL-LFVILSPvGPYFSSGSFTPvslwanpkYIRAW-KGGTGDC 221
Cdd:PRK13356  85 ----RFDPDTALYIRPMYWAEDGFASGVAPDPestrfALcLEEAPMP-EPTGFSLTLSP--------FRRPTlEMAPTDA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 222 KMGGNYGASLLAQCEAVENGCQQVLWLYGKDNqITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 301
Cdd:PRK13356 152 KAGCLYPNNARALREARSRGFDNALVLDMLGN-VAETATSNVF---MVKDGV--VFTPVPNGTFLNGITRQRVIALLRED 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 161016828 302 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK13356 226 G-VTVVETTLTYEDFLEA------DEVFSTGNYSKVVPVTRF 260
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
81-343 5.31e-07

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 50.74  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  81 IHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAvrttlpmfdkeellkcilQLLQIDqewVPYS----- 155
Cdd:PRK07544  25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSA------------------ELLDFE---IPYSvaeid 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 156 --TSASL--------YIRPT-FIGTEpSLGVKKPSKALLFVILS-PVGPYFSS-----GSFTPVSLWANPkyirAWKGGT 218
Cdd:PRK07544  79 aaKKETLaangltdaYVRPVaWRGSE-MMGVSAQQNKIHLAIAAwEWPSYFDPeakmkGIRLDIAKWRRP----DPETAP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 219 GDCKMGGNYGASLLAQCEAVENGCQQVLWL-YgkDNQITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRQSILEL 297
Cdd:PRK07544 154 SAAKAAGLYMICTISKHAAEAKGYADALMLdY--RGYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIEL 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 161016828 298 AQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK07544 226 AKRRG-IEVVERHIMPEELAGF------SECFLTGTAAEVTPVSEI 264
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
90-343 3.17e-06

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 48.41  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  90 YAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpystSASLYIR---- 163
Cdd:PRK12479  29 YGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAksILLTIPL-TVDEMEEAVLQTLQKNE-------YADAYIRlivs 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 164 --PTFIGTEPSlGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWA---NPKYIrawkggtgDCKMGG-NYGASLLAQCEA 237
Cdd:PRK12479  96 rgKGDLGLDPR-SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASrrnTPDAL--------DPRIKSmNYLNNVLVKIEA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 238 VENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLA 317
Cdd:PRK12479 167 AQAGVLEALML-NQQGYVCEGSGDNVF---VVKDGK--VLTPPSYLGALEGITRNSVIELCERLS-IPCEERPFTRHDVY 239
                        250       260
                 ....*....|....*....|....*.
gi 161016828 318 TAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK12479 240 VA------DEVFLTGTAAELIPVVKV 259
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
232-343 9.94e-06

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 46.85  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 232 LAQCEAVENGCQQVlWLYGkDNQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHL 311
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WMVD-DGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPF 230
                         90       100       110
                 ....*....|....*....|....*....|..
gi 161016828 312 TmddLATALEgnrVKEMFGSGTACVVCPVSDI 343
Cdd:PRK06680 231 T---LQEAYA---AREAFITAASSFVFPVVQI 256
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
226-340 1.91e-05

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 46.16  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRQSILELAQQWGEF 304
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161016828 305 K----VCERHLTMDdlatalEGNRVKEMFGSGTACVVCPV 340
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
PRK07546 PRK07546
hypothetical protein; Provisional
254-319 2.96e-05

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 44.58  E-value: 2.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161016828 254 QITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRQSILElaqqwgEFKVCERHLTMDDLATA 319
Cdd:PRK07546 136 EVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSA 191
PRK07849 PRK07849
aminodeoxychorismate lyase;
95-319 1.42e-03

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 40.33  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828  95 FEGLKAFRGvdnKIRLFRPDLnmDRMCRSAVRTTLPMFDKEELLKCILQLLQidqEWvpYSTSASLYIRPTFigtepSLG 174
Cdd:PRK07849  42 FETLLVRDG---RPCNLEAHL--ERLARSAALLDLPEPDLDRWRRAVELAIE---EW--RAPEDEAALRLVY-----SRG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161016828 175 VKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPkyiRAWKGGTGDCK---MGG----NYGASLLAQCEAVENGCQQVLW 247
Cdd:PRK07849 107 RESGGAPTAWVTVSPVPERVARARREGVSVITLD---RGYPSDAAERApwlLAGaktlSYAVNMAALRYAARRGADDVIF 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161016828 248 LYGkDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATA 319
Cdd:PRK07849 184 TST-DGYVLEGPTSTVVIA---TDDR--LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
 
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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