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Conserved domains on  [gi|296010900|ref|NP_001171562|]
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branched-chain-amino-acid aminotransferase, cytosolic isoform 2 [Homo sapiens]

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
32-341 6.00e-114

branched-chain amino acid aminotransferase; Provisional


The actual alignment was detected with superfamily member PRK13357:

Pssm-ID: 237363  Cd Length: 356  Bit Score: 334.81  E-value: 6.00e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  32 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 95
Cdd:PRK13357   7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  96 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 153
Cdd:PRK13357  86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 154 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 232
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 233 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 312
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
                        330       340
                 ....*....|....*....|....*....
gi 296010900 313 IHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
 
Name Accession Description Interval E-value
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
32-341 6.00e-114

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 334.81  E-value: 6.00e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  32 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 95
Cdd:PRK13357   7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  96 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 153
Cdd:PRK13357  86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 154 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 232
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 233 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 312
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
                        330       340
                 ....*....|....*....|....*....
gi 296010900 313 IHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
80-338 1.33e-98

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: 292.95  E-value: 1.33e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  80 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 122
Cdd:cd01557    1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 123 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 202
Cdd:cd01557   81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 203 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:cd01557  159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296010900 283 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 338
Cdd:cd01557  233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
68-346 2.97e-78

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: 242.36  E-value: 2.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900   68 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 110
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  111 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 189
Cdd:TIGR01123  81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  190 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 268
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  269 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 346
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
68-341 5.87e-54

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: 178.84  E-value: 5.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  68 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 114
Cdd:COG0115    4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 115 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 193
Cdd:COG0115   83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 194 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 273
Cdd:COG0115  155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010900 274 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:COG0115  228 ISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
95-306 3.55e-25

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: 101.28  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900   95 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 173
Cdd:pfam01063  36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  174 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 253
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 296010900  254 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
32-341 6.00e-114

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 334.81  E-value: 6.00e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  32 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 95
Cdd:PRK13357   7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  96 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 153
Cdd:PRK13357  86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 154 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 232
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 233 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 312
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
                        330       340
                 ....*....|....*....|....*....
gi 296010900 313 IHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
80-338 1.33e-98

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: 292.95  E-value: 1.33e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  80 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 122
Cdd:cd01557    1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 123 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 202
Cdd:cd01557   81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 203 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:cd01557  159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296010900 283 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 338
Cdd:cd01557  233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
68-346 2.97e-78

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: 242.36  E-value: 2.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900   68 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 110
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  111 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 189
Cdd:TIGR01123  81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  190 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 268
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  269 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 346
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
95-312 8.97e-58

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: 187.81  E-value: 8.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  95 FDKEELLECIQQLVKLdqewvpySTSASLYIRPTFIGTEPSLGV--KKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPK 172
Cdd:cd00449   44 YDREELREALKELVAA-------NNGASLYIRPLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 173 YVRAWKGGTGDCKMGGNYGSSLfAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYWineDGEeeLATPPLDGIILPGV 252
Cdd:cd00449  116 RRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAGADEALLLDDNGY-VTEGSASNVFIVK---DGE--LVTPPLDGGILPGI 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 253 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGET 312
Cdd:cd00449  189 TRDSVIELAKELG-IKVEERPISLDELYAA------DEVFLTGTAAEVTPVTEIDGRGIG 241
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
68-341 5.87e-54

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: 178.84  E-value: 5.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  68 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 114
Cdd:COG0115    4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 115 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 193
Cdd:COG0115   83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 194 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 273
Cdd:COG0115  155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010900 274 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:COG0115  228 ISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
43-349 1.79e-42

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 151.92  E-value: 1.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 97
Cdd:PLN02782  71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGlkayrkedgnillfrpeenairmrn 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  98 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 165
Cdd:PLN02782 151 gaermcmpaptvEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGV-API 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL------YGEdhqitEVGTMNLFLYWINedgeeEL 239
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvhkkYLE-----EVSSCNIFIVKDN-----VI 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 240 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPtmE 319
Cdd:PLN02782 300 STPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYG--E 370
                        330       340       350
                 ....*....|....*....|....*....|...
gi 296010900 320 NGPKLASRIL-SKLTDIQYGREES--DWTIVLS 349
Cdd:PLN02782 371 GGFGTVSQQLyTVLTSLQMGLIEDnmNWTVELS 403
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
47-348 9.99e-39

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 140.84  E-value: 9.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  47 LVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK----------------------------- 97
Cdd:PLN03117  25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGlkayrtedgritlfrpdqnalrmqtgadr 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  98 --------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYF--SSGtfnpVSL 167
Cdd:PLN03117 105 lcmtppslEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkaSSG----LNL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 168 WANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLYWINedgeeELATPPLDG 246
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFILKGN-----IVSTPPTSG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 247 IILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENGpkLAS 326
Cdd:PLN03117 256 TILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LST 326
                        330       340
                 ....*....|....*....|....
gi 296010900 327 RILSKLTDIQYGREESD--WTIVL 348
Cdd:PLN03117 327 KLHLILTNIQMGVVEDKkgWMVEI 350
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
43-343 2.08e-31

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 122.14  E-value: 2.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 97
Cdd:PLN02259  57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGtkayrkengklllfrpdhnairmkl 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  98 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPV 165
Cdd:PLN02259 137 gaermlmpspsvDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYG-EDHQITEVGTMNLFLYwinedGEEELATPPL 244
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 245 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 324
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
                        330
                 ....*....|....*....
gi 296010900 325 ASRILSKLTDIQYGREESD 343
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
43-349 1.92e-29

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 116.35  E-value: 1.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYA----------------VEVFDKE-------- 98
Cdd:PLN02883  53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGqgliegmkayrgedgrILLFRPElnamrmki 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  99 -------------ELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 165
Cdd:PLN02883 133 gaermcmhspsvhQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGED-HQITEVGTMNLFLYWINedgeeELATPPL 244
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGN-----IIVTPAT 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 245 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 324
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
                        330       340
                 ....*....|....*....|....*..
gi 296010900 325 ASRILSKLTDIQYG--REESDWTIVLS 349
Cdd:PLN02883 358 TQQLRSILLGIQTGsiQDTKDWVLQIA 384
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
95-306 3.55e-25

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: 101.28  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900   95 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 173
Cdd:pfam01063  36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  174 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 253
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 296010900  254 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
PRK06606 PRK06606
branched-chain amino acid transaminase;
95-344 8.72e-20

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 88.28  E-value: 8.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  95 FDKEELLECIQQLVKLDQewvpystSASLYIRP-TFIGTEpSLGV---KKPTKALLFVLlsPVGPYFSSGTFNP-----V 165
Cdd:PRK06606  74 YSVDELMEAQREVVRKNN-------LKSAYIRPlVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWA----NPKYVRAwkggtgdcKMGGNYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFlywINEDGEeeL 239
Cdd:PRK06606 144 SSWTrhapNSIPTRA--------KASGNYLNSILAKTEARRNGYDEALLL---DVEgyVSEGSGENIF---IVRDGV--L 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 240 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTME 319
Cdd:PRK06606 208 YTPPLTSSILEGITRDTVITLAKDLG-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREV----DGRQIGNGK 276
                        250       260
                 ....*....|....*....|....*..
gi 296010900 320 NGPkLASRILSKLTDIQYGREE--SDW 344
Cdd:PRK06606 277 RGP-ITEKLQSAYFDIVRGRTEkyAHW 302
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
95-306 3.26e-13

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: 68.78  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900  95 FDKEELLECIQQLVKLDQewvpySTSASLYIRPTFiGTEP-SLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPky 173
Cdd:cd01558   61 YTREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVP-- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 174 VRAWkggtGDCKM-GGNYGSSLFAQCEAVDNGCQQVlWLYGEDHQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGV 252
Cdd:cd01558  133 DIRW----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGI 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296010900 253 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:cd01558  203 TRATVIELAKELG-IPVEERPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
189-306 7.74e-10

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 59.11  E-value: 7.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGe 266
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG- 224
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 296010900 267 FKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:PRK08320 225 IPVREELFTLHDLYTA------DEVFLTGTAAEVIPVVKV 258
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
189-290 6.56e-09

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 55.78  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRRCILDLAHQWGEfK 268
Cdd:cd01559  127 NYLENVLAKREARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGY-A 199
                         90       100
                 ....*....|....*....|....*
gi 296010900 269 VSERYLTMDDLTTALE---GNRVRE 290
Cdd:cd01559  200 VDERPLRLEDLLAADEaflTNSLLG 224
PRK07546 PRK07546
hypothetical protein; Provisional
211-292 9.45e-06

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 46.12  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 211 LYGEDHQITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRRCILDlahqwgEFKVSERYLTMDDLTTA---LEGNR 287
Cdd:PRK07546 130 LLNERGEVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSAraiWVGNS 199

                 ....*
gi 296010900 288 VREMF 292
Cdd:PRK07546 200 LRGLI 204
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
204-306 6.29e-05

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 44.20  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 204 GCQQVLWLygeDH--QITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTT 281
Cdd:PRK07544 176 GYADALML---DYrgYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVERHIMPEELAG 245
                         90       100
                 ....*....|....*....|....*
gi 296010900 282 AlegnrvREMFGSGTACVVCPVSDI 306
Cdd:PRK07544 246 F------SECFLTGTAAEVTPVSEI 264
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
200-313 8.01e-05

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 43.77  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 200 AVDNGCQQVlWlYGEDHQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDl 279
Cdd:PRK06680 163 AKEAGAQEA-W-MVDDGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPFTLQE- 234
                         90       100       110
                 ....*....|....*....|....*....|....
gi 296010900 280 ttALEgnrVREMFGSGTACVVCPVSDIlyKGETI 313
Cdd:PRK06680 235 --AYA---AREAFITAASSFVFPVVQI--DGKQI 261
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
189-303 2.48e-03

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 39.23  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRRCILDLAHQWGEF 267
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 296010900 268 K----VSERYLTMDdlttalEGNRVREMFGSGTACVVCPV 303
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
PRK07849 PRK07849
aminodeoxychorismate lyase;
239-282 5.47e-03

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 38.02  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 296010900 239 LATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:PRK07849 206 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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