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Conserved domains on  [gi|384468320|gb|EIE52756|]
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D-alanine aminotransferase [Citreicella sp. 357]

Protein Classification

aminotransferase class IV( domain architecture ID 1051)

aminotransferase class IV is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE), similar to Staphylococcus D-alanine aminotransferase

Gene Ontology:  GO:0030170
PubMed:  31989227

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_IV super family cl00224
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 1-286 4.57e-134

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


The actual alignment was detected with superfamily member PRK06680:

Pssm-ID: 444764 [Multi-domain]  Cd Length: 286  Bit Score: 380.82  E-value: 4.57e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   1 MSRTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVD 80
Cdd:PRK06680   1 MKRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  81 LNDISEGLIYLQVTRGApGDRDFAFPdPETTEPTLVLFTQNKPGLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSM 160
Cdd:PRK06680  81 RNRVREGLVYLQVTRGV-ARRDHVFP-AADVKPSVVVFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 161 GKMMARKAGADDAWMVEDGFVTEGTSNNAYIV-KDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREA 239
Cdd:PRK06680 159 AKQAAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 384468320 240 DEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLAESLKAA 286
Cdd:PRK06680 239 REAFITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYEEFARLTA 285
 
Name Accession Description Interval E-value
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 1-286 4.57e-134

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 380.82  E-value: 4.57e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   1 MSRTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVD 80
Cdd:PRK06680   1 MKRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  81 LNDISEGLIYLQVTRGApGDRDFAFPdPETTEPTLVLFTQNKPGLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSM 160
Cdd:PRK06680  81 RNRVREGLVYLQVTRGV-ARRDHVFP-AADVKPSVVVFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 161 GKMMARKAGADDAWMVEDGFVTEGTSNNAYIV-KDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREA 239
Cdd:PRK06680 159 AKQAAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 384468320 240 DEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLAESLKAA 286
Cdd:PRK06680 239 REAFITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYEEFARLTA 285
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 6-278 2.09e-121

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: 348.05  E-value: 2.09e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   6 YLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDIS 85
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  86 EGLIYLQVTRGApGDRDFAFPdpETTEPTLVLFTQnKPGLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSMGKMMA 165
Cdd:cd01558   81 EGDVYIQVTRGV-GPRGHDFP--KCVKPTVVIITQ-PLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 166 RKAGADDAWMVE-DGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFL 244
Cdd:cd01558  157 KEAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFL 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 384468320 245 TSASAFVMPVVEIDGASVGTGTPGPVAARLREIY 278
Cdd:cd01558  237 TSTTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 3-280 8.53e-106

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: 309.04  E-value: 8.53e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   3 RTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLN 82
Cdd:COG0115    1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  83 DISEGLIYLQVTRGApGDRDFafpDPETTEPTLVLFTQNKPgLSDNPVAKKGIKVISIDDIRW---GRRDIKTVQLLYPS 159
Cdd:COG0115   81 GLEDGYIRPQVTRGV-GGRGV---FAEEYEPTVIIIASPLP-AYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 160 MGKMMARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEARE 238
Cdd:COG0115  156 LAKQEAKEAGADEALLLdTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYT 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 384468320 239 ADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLA 280
Cdd:COG0115  236 ADEVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTD 277
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 5-276 1.80e-78

D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130191  Cd Length: 276  Bit Score: 239.25  E-value: 1.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320    5 VYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDI 84
Cdd:TIGR01121   2 VLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   85 SEGLIYLQVTRG-APgdRDFAFPDPETtEPTLVLFTQNKPGLSDNPVakKGIKVISIDDIRWGRRDIKTVQLLYPSMGKM 163
Cdd:TIGR01121  82 NTGHVYFQVTRGvAP--RNHQFPAGTV-KPVITAYTKEVPRPEENLE--KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  164 MARKAGADDAWMVEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAF 243
Cdd:TIGR01121 157 EAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVF 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 384468320  244 LTSASAFVMPVVEIDGASVGTGTPGPVAARLRE 276
Cdd:TIGR01121 237 VSSTTAEITPVIEIDGQQIGDGKPGPWTRQLQK 269
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 31-257 2.12e-49

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: 162.91  E-value: 2.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   31 GVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDISEGLIYLQVTRGaPGDRDFAFPDPet 110
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRG-PGGFGLPTSDP-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  111 tepTLVLFTQNKPgLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSMGKMMARKAGADDAWMV-EDGFVTEGTSNNA 189
Cdd:pfam01063  78 ---TLAIFVSALP-PPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNV 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468320  190 YIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEI 257
Cdd:pfam01063 154 FLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 1-286 4.57e-134

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 380.82  E-value: 4.57e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   1 MSRTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVD 80
Cdd:PRK06680   1 MKRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  81 LNDISEGLIYLQVTRGApGDRDFAFPdPETTEPTLVLFTQNKPGLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSM 160
Cdd:PRK06680  81 RNRVREGLVYLQVTRGV-ARRDHVFP-AADVKPSVVVFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 161 GKMMARKAGADDAWMVEDGFVTEGTSNNAYIV-KDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREA 239
Cdd:PRK06680 159 AKQAAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 384468320 240 DEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLAESLKAA 286
Cdd:PRK06680 239 REAFITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYEEFARLTA 285
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 6-278 2.09e-121

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: 348.05  E-value: 2.09e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   6 YLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDIS 85
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  86 EGLIYLQVTRGApGDRDFAFPdpETTEPTLVLFTQnKPGLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSMGKMMA 165
Cdd:cd01558   81 EGDVYIQVTRGV-GPRGHDFP--KCVKPTVVIITQ-PLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 166 RKAGADDAWMVE-DGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFL 244
Cdd:cd01558  157 KEAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFL 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 384468320 245 TSASAFVMPVVEIDGASVGTGTPGPVAARLREIY 278
Cdd:cd01558  237 TSTTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 3-280 8.53e-106

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: 309.04  E-value: 8.53e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   3 RTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLN 82
Cdd:COG0115    1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  83 DISEGLIYLQVTRGApGDRDFafpDPETTEPTLVLFTQNKPgLSDNPVAKKGIKVISIDDIRW---GRRDIKTVQLLYPS 159
Cdd:COG0115   81 GLEDGYIRPQVTRGV-GGRGV---FAEEYEPTVIIIASPLP-AYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 160 MGKMMARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEARE 238
Cdd:COG0115  156 LAKQEAKEAGADEALLLdTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYT 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 384468320 239 ADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLA 280
Cdd:COG0115  236 ADEVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTD 277
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 23-278 1.20e-79

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 241.35  E-value: 1.20e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  23 DRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDISEGLIYLQVTRGApGDRD 102
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGV-GGLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 103 FAFPDPetTEPTLVLFTQnkPGLSDNPVAKKGIKVISIDDIR----WGRRDIKTVQLLYPSMGKMMARKAGADDAWMV-E 177
Cdd:cd00449   80 VAPPPS--PEPTFVVFAS--PVGAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLdD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 178 DGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEI 257
Cdd:cd00449  156 NGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEI 235

                        250       260
                 ....*....|....*....|.
gi 384468320 258 DGASVGTGTPGPVAARLREIY 278
Cdd:cd00449  236 DGRGIGDGKPGPVTRKLRELL 256
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 5-276 1.80e-78

D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130191  Cd Length: 276  Bit Score: 239.25  E-value: 1.80e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320    5 VYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDI 84
Cdd:TIGR01121   2 VLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   85 SEGLIYLQVTRG-APgdRDFAFPDPETtEPTLVLFTQNKPGLSDNPVakKGIKVISIDDIRWGRRDIKTVQLLYPSMGKM 163
Cdd:TIGR01121  82 NTGHVYFQVTRGvAP--RNHQFPAGTV-KPVITAYTKEVPRPEENLE--KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  164 MARKAGADDAWMVEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAF 243
Cdd:TIGR01121 157 EAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVF 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 384468320  244 LTSASAFVMPVVEIDGASVGTGTPGPVAARLRE 276
Cdd:TIGR01121 237 VSSTTAEITPVIEIDGQQIGDGKPGPWTRQLQK 269
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 1-276 1.89e-51

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 170.44  E-value: 1.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   1 MSRTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVD 80
Cdd:PRK08320   1 MEQLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  81 LNDISEGLIYLQVTRGApGDRDFafpDPE-TTEPTLVLFTQNKPGLSDNpVAKKGIKVISIDdIRWGRRD-----IKTVQ 154
Cdd:PRK08320  81 KNNLRDAYIRLVVSRGV-GDLGL---DPRkCPKPTVVCIAEPIGLYPGE-LYEKGLKVITVS-TRRNRPDalspqVKSLN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 155 LLYPSMGKMMARKAGADDAWMVED-GFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSI 233
Cdd:PRK08320 155 YLNNILAKIEANLAGVDEAIMLNDeGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 384468320 234 DEAREADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLRE 276
Cdd:PRK08320 235 HDLYTADEVFLTGTAAEVIPVVKVDGRVIGDGKPGPITKKLLE 277
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 31-257 2.12e-49

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: 162.91  E-value: 2.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   31 GVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDISEGLIYLQVTRGaPGDRDFAFPDPet 110
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRG-PGGFGLPTSDP-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  111 tepTLVLFTQNKPgLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSMGKMMARKAGADDAWMV-EDGFVTEGTSNNA 189
Cdd:pfam01063  78 ---TLAIFVSALP-PPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNV 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384468320  190 YIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEI 257
Cdd:pfam01063 154 FLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 23-278 5.74e-47

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: 157.47  E-value: 5.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  23 DRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPaafgDLLEIHRKLVDL---NDISEGLIYLQVTRGaPG 99
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEP----DLPRLRAALESLlaaNDIDEGRIRLILSRG-PG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 100 DRDFAfpDPETTEPTLVLFTQNKPGLSDNpvakKGIKVISID---DIRWGRRDIKTVQLLYPSMGKMMARKAGADDAWMV 176
Cdd:cd01559   76 GRGYA--PSVCPGPALYVSVIPLPPAWRQ----DGVRLITCPvrlGEQPLLAGLKHLNYLENVLAKREARDRGADEALFL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 177 -EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVV 255
Cdd:cd01559  150 dTDGRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVT 229

                        250       260
                 ....*....|....*....|...
gi 384468320 256 EIDGasvGTGTPGPVAARLREIY 278
Cdd:cd01559  230 AIDD---HDGPPGPLTRALRELL 249
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
5-278 3.67e-46

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 157.04  E-value: 3.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   5 VYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDI 84
Cdd:PRK12479   6 IYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNEY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  85 SEGLIYLQVTRGaPGDRDFafpDPETTEPTLVLFTQNKPGLSDNPVAKKGIKVISIDDirwgRRD--------IKTVQLL 156
Cdd:PRK12479  86 ADAYIRLIVSRG-KGDLGL---DPRSCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVAS----RRNtpdaldprIKSMNYL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 157 YPSMGKMMARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDE 235
Cdd:PRK12479 158 NNVLVKIEAAQAGVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHD 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 384468320 236 AREADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIY 278
Cdd:PRK12479 238 VYVADEVFLTGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEF 280
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 3-285 5.86e-44

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 150.94  E-value: 5.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   3 RTVYLNGEYLPETEAK--VSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVD 80
Cdd:PRK12400   5 RFVLWNDAVIDTTKQKtyIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  81 LNDISE-GLIYLQVTRGAPGdRDFAFPdpETTEPTLVLFTQNK--PGLSdnpvAKKGIKVISIDDIRWGRRDIKTVQLLY 157
Cdd:PRK12400  85 NNNFHEdGTIYLQVSRGVQA-RTHTFS--YDVPPTIYAYITKKerPALW----IEYGVRAISEPDTRWLRCDIKSLNLLP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 158 PSMGKMMARKAGADDAWMVEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAR 237
Cdd:PRK12400 158 NILAATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVY 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 384468320 238 EADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLAESLKA 285
Cdd:PRK12400 238 QADECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQS 285
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
 6-278 9.61e-43

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: 148.28  E-value: 9.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320    6 YLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVL---GGKLIDFAG-HARRLERSLAELDIKKPAAFGDLLEIHRKLVDL 81
Cdd:TIGR01122   1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYdtdKGPAIFRLKeHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   82 NDISEGLIYLQVTRGapgDRDFAFPDPETTEPTLVLFTQNKPGLSDNPVAKKGIKVISIDdirWGRRDIKTVQL------ 155
Cdd:TIGR01122  81 NNLRSAYIRPLVFRG---DGDLGLNPRAGYKPDVIIAAWPWGAYLGEEALEKGIDAKVSS---WRRNAPNTIPTaakagg 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  156 LYPS--MGKMMARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFS 232
Cdd:TIGR01122 155 NYLNslLAKSEARRHGYDEAILLdVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPIS 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 384468320  233 IDEAREADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIY 278
Cdd:TIGR01122 235 REELYTADEAFFTGTAAEITPIREVDGRKIGNGRRGPVTKKLQEAF 280
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 5-284 8.63e-38

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 134.71  E-value: 8.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   5 VYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGK--LIDfaGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLN 82
Cdd:PRK07650   2 IYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHpfLLD--DHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  83 DISEGLIYLQVTRGaPGDRDFaFPDPeTTEPTLVLFTqnKP-GLSDNPVAKKGIKVISIDDIRWGRRDIKTVQLLYPSMG 161
Cdd:PRK07650  80 GLENAYVRFNVSAG-IGEIGL-QTEM-YEEPTVIVYM--KPlAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 162 KmmaRKAGADDA----WMVEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAR 237
Cdd:PRK07650 155 K---REIGNDPNkegiFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELL 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 384468320 238 EADEAFLTSASAFVMPVVEIDGASVGtGTPGPVAARLREIYLAESLK 284
Cdd:PRK07650 232 SADEVFVTNSIQEIVPLTRIEERDFP-GKVGMVTKRLQNLYEMQREK 277
PRK06606 PRK06606
branched-chain amino acid transaminase;
2-280 3.82e-35

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 128.34  E-value: 3.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   2 SRTVYLNGEYLPETEAKVSIFDRAFLMADGVYEVT----SVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRK 77
Cdd:PRK06606   6 AGYIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIraydTPKGPAIFRLREHTKRLFNSAKILRMEIPYSVDELMEAQRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  78 LVDLNDISEGLIylqvtrgapgdRDFAF-------PDPETTEPTLVLFTQNKPGLSDNPVAKKGIKV-ISiddiRWGRRD 149
Cdd:PRK06606  86 VVRKNNLKSAYI-----------RPLVFvgdeglgVRPHGLPTDVAIAAWPWGAYLGEEALEKGIRVkVS----SWTRHA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 150 IKTVQL------LYPS--MGKMMARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAR 220
Cdd:PRK06606 151 PNSIPTrakasgNYLNsiLAKTEARRNGYDEALLLdVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAK 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 221 EAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEIDGASVGTGTPGPVAARLREIYLA 280
Cdd:PRK06606 231 DLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGKRGPITEKLQSAYFD 290
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 162-278 3.15e-28

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: 109.59  E-value: 3.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 162 KMMARKAGADDA-WM-VEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREA 239
Cdd:cd01557  153 QKEAAEKGYDQAlWLdGAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEA 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 384468320 240 DEAFLTSASAFVMPVVEID--GASVGTGTPGPVAARLREIY 278
Cdd:cd01557  233 DEVFATGTAAVVTPVGEIDyrGKEPGEGEVGPVTKKLYDLL 273
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 31-281 2.54e-23

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 97.39  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  31 GVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDISEGLIYLQVTRGaPGDrdFAFPDPET 110
Cdd:PLN02845  69 GVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGSLRYWLSAG-PGG--FSLSPSGC 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 111 TEPTL-VLFTQNKPGlsdnPVAKKGIKVISID-DIRWGR-RDIKTVQLLYPSMGKMMARKAGADDA-WMVEDGFVTEGTS 186
Cdd:PLN02845 146 SEPAFyAVVIEDTYA----QDRPEGVKVVTSSvPIKPPQfATVKSVNYLPNALSQMEAEERGAFAGiWLDEEGFVAEGPN 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 187 NN-AYIVKDGKIITRNLgTDILHGITRAAVLACAREAQ-----MAVEERPFSIDEAREADEAFLTSASAFVMPVVEIDGA 260
Cdd:PLN02845 222 MNvAFLTNDGELVLPPF-DKILSGCTARRVLELAPRLVspgdlRGVKQRKISVEEAKAADEMMLIGSGVPVLPIVSWDGQ 300

                        250       260
                 ....*....|....*....|.
gi 384468320 261 SVGTGTPGPVAARLREIYLAE 281
Cdd:PLN02845 301 PIGDGKVGPITLALHDLLLDD 321
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 5-281 3.39e-23

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 96.20  E-value: 3.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320   5 VYLNGEYLPETEAKVSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAAFGDLLEIHRKLVDLNDI 84
Cdd:PRK07544  11 IWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  85 SEGLIYLQVTRGAPgdrDFAFPDPETTePTLVLFTQNKPGLSDNPVAKKGIKvisIDDIRWGRRDIKTVQL------LYP 158
Cdd:PRK07544  91 TDAYVRPVAWRGSE---MMGVSAQQNK-IHLAIAAWEWPSYFDPEAKMKGIR---LDIAKWRRPDPETAPSaakaagLYM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 159 --SMGKMMARKAGADDAWMVE-DGFVTEGTSNNAYIVKDGKIITrNLGTDILHGITRAAVLACAREAQMAVEERPFSIDE 235
Cdd:PRK07544 164 icTISKHAAEAKGYADALMLDyRGYVAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIELAKRRGIEVVERHIMPEE 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 384468320 236 AREADEAFLTSASAFVMPVVEIDGASVgtgTPGPVAARLREIYLAE 281
Cdd:PRK07544 243 LAGFSECFLTGTAAEVTPVSEIGEYRF---TPGAITRDLMDDYEAL 285
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 19-277 1.56e-22

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 93.75  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  19 VSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIkkPAAFGDLLEIHRKLVDLNDiSEGLIYLQVTRGAp 98
Cdd:PRK06092  12 LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAI--PLDDWAQLEQEMKQLAAEL-ENGVLKVIISRGS- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  99 GDRDFAfPDPETtEPTLVLFTqnkpglSDNPV-----AKKGIKViSIDDIRWGRR----DIKTVQLLYPSMGKMMARKAG 169
Cdd:PRK06092  88 GGRGYS-PAGCA-APTRILSV------SPYPAhysrwREQGITL-ALCPTRLGRNpllaGIKHLNRLEQVLIRAELEQTE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 170 ADDAWMVE-DGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSAs 248
Cdd:PRK06092 159 ADEALVLDsEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNS- 237

                        250       260
                 ....*....|....*....|....*....
gi 384468320 249 afVMPVVEIDGASVGTGTPGPVAARLREI 277
Cdd:PRK06092 238 --LMPVWPVRAIGETSYSSGTLTRYLQPL 264
PRK07849 PRK07849
aminodeoxychorismate lyase;
19-287 2.73e-21

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 90.79  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  19 VSIFDRAFLMADGVYEVTSVLGGKLIDFAGHARRLERSLAELDIKKPAafgdlLEIHRKLVDL------NDISEGLIYLQ 92
Cdd:PRK07849  28 LHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEPD-----LDRWRRAVELaieewrAPEDEAALRLV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  93 VTRGAPGdrdfafpdpeTTEPTLVLFTQNKPGlSDNPVAKKGIKVISID-----DIR----WGRRDIKTVqllypSMGKM 163
Cdd:PRK07849 103 YSRGRES----------GGAPTAWVTVSPVPE-RVARARREGVSVITLDrgypsDAAerapWLLAGAKTL-----SYAVN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 164 M-----ARKAGADDAWMV-EDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAR 237
Cdd:PRK07849 167 MaalryAARRGADDVIFTsTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLF 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 384468320 238 EADEAFLTSASAFVMPVVEIDgasvgtGTPGPVAARLREIylAESLKAAL 287
Cdd:PRK07849 247 AADGVWLVSSVRLAARVHTLD------GRPLPRDPLADEL--TELVDAAI 288
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
156-278 7.12e-20

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 86.93  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 156 LYPSMGKMM--ARKAGADDAWMVE-DGFVTEGTSNNAYIVKDGKIIT--RNlGTdILHGITRAAVLACAREAQMAVEERP 230
Cdd:PRK13356 156 LYPNNARALreARSRGFDNALVLDmLGNVAETATSNVFMVKDGVVFTpvPN-GT-FLNGITRQRVIALLREDGVTVVETT 233

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 384468320 231 FSIDEAREADEAFLTSASAFVMPVVEIDGASVgtgTPGPVAARLREIY 278
Cdd:PRK13356 234 LTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL---QPGPVTRRARELY 278
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
 163-280 2.72e-17

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 80.58  E-value: 2.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 163 MMARKAGADDA-W--MVEDGFVTE-GTSNNAYIVKDGKIITRNLGTdILHGITRAAVLACAREAQMAVEERPFSIDEARE 238
Cdd:PRK13357 209 AEAKEKGCDQVlYldAVEHTYIEEvGGMNFFFITKDGTVTPPLSGS-ILPGITRDSLLQLAEDLGLTVEERPVSIDEWQA 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384468320 239 A------DEAFLTSASAFVMPVVEIDGA----SVGTGTPGPVAARLREIYLA 280
Cdd:PRK13357 288 DaasgefTEAFACGTAAVITPIGGIKYKdkefVIGDGEVGPVTQKLYDELTG 339
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
 165-276 1.55e-16

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: 78.26  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320  165 ARKAGADDA-WM--VEDGFVTE-GTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREAD 240
Cdd:TIGR01123 170 AAEQGCDQVvYLdpVEHTYIEEvGAMNFFFITGDGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERRIDIDELKAFV 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 384468320  241 EA----FLTSASAFVMPVVEI----DGASVGTGTPGPVAARLRE 276
Cdd:TIGR01123 250 EAgeivFACGTAAVITPVGEIqhggKEVVFASGQPGEVTKALYD 293
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 180-274 2.64e-12

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 66.41  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 180 FVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEI-- 257
Cdd:PLN02782 282 YLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSIty 361

                         90
                 ....*....|....*....
gi 384468320 258 --DGASVGTGTPGPVAARL 274
Cdd:PLN02782 362 kgKRVSYGEGGFGTVSQQL 380
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 176-254 1.21e-07

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 52.42  E-value: 1.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384468320 176 VEDGFVTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPV 254
Cdd:PLN02259 264 VKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPV 342
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 165-254 2.44e-07

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 51.09  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 165 ARKAGADDAWMVEDGF---VTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADE 241
Cdd:PLN03117 213 AKSSGFSDVLFLDAATgknIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEE 292

                         90
                 ....*....|...
gi 384468320 242 AFLTSASAFVMPV 254
Cdd:PLN03117 293 VFCTGTAVVVKAV 305
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 181-257 1.83e-06

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 48.56  E-value: 1.83e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384468320 181 VTEGTSNNAYIVKDGKIITRNLGTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEAFLTSASAFVMPVVEI 257
Cdd:PLN02883 265 IEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSI 341
PRK09266 PRK09266
hypothetical protein; Provisional
 165-281 2.13e-05

hypothetical protein; Provisional


Pssm-ID: 236438  Cd Length: 266  Bit Score: 44.97  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384468320 165 ARKAGADDAWMVE-DGFVTEG-TSNNAYIVKDGKIITRnlgTDILHGITRAAVLACAREAQMAVEERPFSIDEAREADEA 242
Cdd:PRK09266 148 AQRAGFDDALFVDpDGRVSEGaTWNLGFWDGGAVVWPQ---APALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAGA 224

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 384468320 243 FLTSASAFVMPVVEIDGASVGTGTpgPVAARLREIYLAE 281
Cdd:PRK09266 225 FACNAWRGQRAVSAIDDVALPDSH--ALLELLRRAYEAE 261
 
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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