NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488677036|ref|WP_002605809|]
View 

MULTISPECIES: D-amino-acid transaminase [Bacillota]

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

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 4-274 9.69e-104

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 cd01558:

Pssm-ID: 444764 [Multi-domain]  Cd Length: 270  Bit Score: 302.98  E-value: 9.69e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   4 LWKGSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIE 83
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  84 NGYIYLQVTRGDGTlRNHGFSmyEEQQP-VFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQ 162
Cdd:cd01558   81 EGDVYIQVTRGVGP-RGHDFP--KCVKPtVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 163 KKGVSKAIMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:cd01558  158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488677036 242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLY 274
Cdd:cd01558  238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
 
Name Accession Description Interval E-value
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 4-274 9.69e-104

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: 302.98  E-value: 9.69e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   4 LWKGSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIE 83
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  84 NGYIYLQVTRGDGTlRNHGFSmyEEQQP-VFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQ 162
Cdd:cd01558   81 EGDVYIQVTRGVGP-RGHDFP--KCVKPtVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 163 KKGVSKAIMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:cd01558  158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488677036 242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLY 274
Cdd:cd01558  238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 2-279 7.96e-102

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: 298.57  E-value: 7.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036    2 KYLWKGSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNH 81
Cdd:TIGR01121   1 KVLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   82 IENGYIYLQVTRGDgTLRNHGFSMyEEQQPVFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAA 161
Cdd:TIGR01121  81 LNTGHVYFQVTRGV-APRNHQFPA-GTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  162 QKKGVSKAIMVRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 488677036  242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIE 279
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEEKIP 276
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 7-282 1.51e-93

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: 277.84  E-value: 1.51e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:COG0115    7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGLEDGY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTLrnhGFSMyEEQQPVFCGFAQS-STRSEEKMVKGADAITVEDRR---SLMCNVKSLNLLPNCLAKHAAQ 162
Cdd:COG0115   87 IRPQVTRGVGGR---GVFA-EEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRaapGGLGGIKTGNYLNNVLAKQEAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 163 KKGVSKAIMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:COG0115  163 EAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFLT 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488677036 242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIEEKC 282
Cdd:COG0115  243 GTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVRGEA 283
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 7-274 5.87e-83

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 251.00  E-value: 5.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:PRK06680   9 GRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVREGL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTlRNHGFSMyEEQQPVFCGFAQSS--TRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQKK 164
Cdd:PRK06680  89 VYLQVTRGVAR-RDHVFPA-ADVKPSVVVFAKSVdfARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 165 GVSKAIMVRDNIVTEEKSGNIFIV-KDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDT 243
Cdd:PRK06680 167 GAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAA 246

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488677036 244 NSEIVPVIKVNDIIIGNGARGEITKKIQMLY 274
Cdd:PRK06680 247 SSFVFPVVQIDGKQIGNGKPGPIAKRLREAY 277
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 29-253 1.10e-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: 163.68  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   29 GIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGYIYLQVTRGDGTLRnhgfsmYEE 108
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFG------LPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  109 QQPVFCGFAQSSTRSEEKMVKGADAITV-EDRRSLMCNVKSLNLLPNCLAKHAAQKKGVSKAIMV-RDNIVTEEKSGNIF 186
Cdd:pfam01063  75 SDPTLAIFVSALPPPPESKKKGVISSLVrRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488677036  187 IVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKV 253
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 4-274 9.69e-104

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: 302.98  E-value: 9.69e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   4 LWKGSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIE 83
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  84 NGYIYLQVTRGDGTlRNHGFSmyEEQQP-VFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQ 162
Cdd:cd01558   81 EGDVYIQVTRGVGP-RGHDFP--KCVKPtVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 163 KKGVSKAIMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:cd01558  158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488677036 242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLY 274
Cdd:cd01558  238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 2-279 7.96e-102

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: 298.57  E-value: 7.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036    2 KYLWKGSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNH 81
Cdd:TIGR01121   1 KVLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   82 IENGYIYLQVTRGDgTLRNHGFSMyEEQQPVFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAA 161
Cdd:TIGR01121  81 LNTGHVYFQVTRGV-APRNHQFPA-GTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  162 QKKGVSKAIMVRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 488677036  242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIE 279
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEEKIP 276
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 7-282 1.51e-93

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: 277.84  E-value: 1.51e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:COG0115    7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGLEDGY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTLrnhGFSMyEEQQPVFCGFAQS-STRSEEKMVKGADAITVEDRR---SLMCNVKSLNLLPNCLAKHAAQ 162
Cdd:COG0115   87 IRPQVTRGVGGR---GVFA-EEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRaapGGLGGIKTGNYLNNVLAKQEAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 163 KKGVSKAIMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVT 241
Cdd:COG0115  163 EAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFLT 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488677036 242 DTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIEEKC 282
Cdd:COG0115  243 GTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVRGEA 283
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 21-274 2.00e-84

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: 253.68  E-value: 2.00e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  21 DRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGYIYLQVTRGDGTLrn 100
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGVGGL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 101 hGFSMYEEQQPVFCGFAQSSTRSEEKMVKGADAITVEDRR----SLMCNVKSLNLLPNCLAKHAAQKKGVSKAIMVRDN- 175
Cdd:cd00449   79 -GVAPPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNg 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 176 IVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKVND 255
Cdd:cd00449  158 YVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDG 237

                        250
                 ....*....|....*....
gi 488677036 256 IIIGNGARGEITKKIQMLY 274
Cdd:cd00449  238 RGIGDGKPGPVTRKLRELL 256
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 7-274 5.87e-83

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 251.00  E-value: 5.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:PRK06680   9 GRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVREGL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTlRNHGFSMyEEQQPVFCGFAQSS--TRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQKK 164
Cdd:PRK06680  89 VYLQVTRGVAR-RDHVFPA-ADVKPSVVVFAKSVdfARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 165 GVSKAIMVRDNIVTEEKSGNIFIV-KDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDT 243
Cdd:PRK06680 167 GAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAA 246

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488677036 244 NSEIVPVIKVNDIIIGNGARGEITKKIQMLY 274
Cdd:PRK06680 247 SSFVFPVVQIDGKQIGNGKPGPIAKRLREAY 277
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 4-271 2.84e-68

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 213.73  E-value: 2.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   4 LWKGSFVD--KEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNH 81
Cdd:PRK12400   8 LWNDAVIDttKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  82 I-ENGYIYLQVTRGDGTlRNHGFSMyeEQQPVFCGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHA 160
Cdd:PRK12400  88 FhEDGTIYLQVSRGVQA-RTHTFSY--DVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNILAATK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 161 AQKKGVSKAIMVRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMV 240
Cdd:PRK12400 165 AERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFF 244

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488677036 241 TDTNSEIVPVIKVNDIIIGNGARGEITKKIQ 271
Cdd:PRK12400 245 TGTTIEILPMTHLDGTAIQDGQVGPITKMLQ 275
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 7-270 3.51e-68

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 213.19  E-value: 3.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:PRK08320   9 GEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNNLRDAY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTLrnhGFSMYEEQQP-VFCGFAQSSTRSEEKMVKGADAITVEDRR----SLMCNVKSLNLLPNCLAKHAA 161
Cdd:PRK08320  89 IRLVVSRGVGDL---GLDPRKCPKPtVVCIAEPIGLYPGELYEKGLKVITVSTRRnrpdALSPQVKSLNYLNNILAKIEA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 162 QKKGVSKAIMVRDNIVTEEKSG-NIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMV 240
Cdd:PRK08320 166 NLAGVDEAIMLNDEGYVAEGTGdNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVFL 245

                        250       260       270
                 ....*....|....*....|....*....|
gi 488677036 241 TDTNSEIVPVIKVNDIIIGNGARGEITKKI 270
Cdd:PRK08320 246 TGTAAEVIPVVKVDGRVIGDGKPGPITKKL 275
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
 7-281 2.80e-61

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: 196.04  E-value: 2.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036    7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNG----VLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHI 82
Cdd:TIGR01122   4 GEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTdkgpAIFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRKNNL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   83 ENGYIYLQVTRGDGTLRNHGFSMYEEQqpVFC-GFAQSSTRSEEKMVKGADAITVEDRR----SLMCNVKSLNLLPNC-L 156
Cdd:TIGR01122  84 RSAYIRPLVFRGDGDLGLNPRAGYKPD--VIIaAWPWGAYLGEEALEKGIDAKVSSWRRnapnTIPTAAKAGGNYLNSlL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  157 AKHAAQKKGVSKAIMVRDNIVTEEKSG-NIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHA 235
Cdd:TIGR01122 162 AKSEARRHGYDEAILLDVEGYVAEGSGeNIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 488677036  236 DEVMVTDTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIEEK 281
Cdd:TIGR01122 242 DEAFFTGTAAEITPIREVDGRKIGNGRRGPVTKKLQEAFFDLVTGG 287
PRK06606 PRK06606
branched-chain amino acid transaminase;
1-281 1.97e-50

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 168.02  E-value: 1.97e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   1 MKYLW-KGSFVDKED--IHI---DLHdrgyqFGDGIYEVTHVYNG----VLFALDEHIDRLINSAAFIELNLRHTKDEIA 70
Cdd:PRK06606   6 AGYIWfNGELVPWEDakVHVlthALH-----YGTGVFEGIRAYDTpkgpAIFRLREHTKRLFNSAKILRMEIPYSVDELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  71 AFCRGLVEQNHIENGYIYLQVTRGDGTL--RNHG----FSMYeeqqpvfcGFAQSSTRSEEKMVKGADAITVEDRR---- 140
Cdd:PRK06606  81 EAQREVVRKNNLKSAYIRPLVFVGDEGLgvRPHGlptdVAIA--------AWPWGAYLGEEALEKGIRVKVSSWTRhapn 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 141 SLMCNVK-SLNLLPNCLAKHAAQKKGVSKAIMVRDNIVTEEKSG-NIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQH 218
Cdd:PRK06606 153 SIPTRAKaSGNYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGeNIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488677036 219 NIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIEEK 281
Cdd:PRK06606 233 GIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGKRGPITEKLQSAYFDIVRGR 295
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
7-281 2.10e-50

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 167.82  E-value: 2.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:PRK12479  10 GEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNEYADAY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTLrnhGFSMYEEQQPVFCGFA-QSSTRSEEKMVKGADAITVEDRR----SLMCNVKSLNLLPNCLAKHAA 161
Cdd:PRK12479  90 IRLIVSRGKGDL---GLDPRSCVKPSVIIIAeQLKLFPQEFYDNGLSVVSVASRRntpdALDPRIKSMNYLNNVLVKIEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 162 QKKGVSKAIMV-RDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMV 240
Cdd:PRK12479 167 AQAGVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFL 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488677036 241 TDTNSEIVPVIKVNDIIIGNGARGEITKKIQMLYKSLIEEK 281
Cdd:PRK12479 247 TGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEFKKLTRER 287
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 29-253 1.10e-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: 163.68  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   29 GIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGYIYLQVTRGDGTLRnhgfsmYEE 108
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFG------LPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  109 QQPVFCGFAQSSTRSEEKMVKGADAITV-EDRRSLMCNVKSLNLLPNCLAKHAAQKKGVSKAIMV-RDNIVTEEKSGNIF 186
Cdd:pfam01063  75 SDPTLAIFVSALPPPPESKKKGVISSLVrRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488677036  187 IVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKV 253
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 21-274 3.23e-45

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: 152.85  E-value: 3.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  21 DRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLrHTKDEIAAFCRGLVEQNHIENGYIYLQVTRGDGTLrn 100
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPE-PDLPRLRAALESLLAANDIDEGRIRLILSRGPGGR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 101 hGFSMYEEQQPVFCGFAQSSTRseEKMVKGADAITVEDR---RSLMCNVKSLNLLPNCLAKHAAQKKGVSKAIMVR-DNI 176
Cdd:cd01559   78 -GYAPSVCPGPALYVSVIPLPP--AWRQDGVRLITCPVRlgeQPLLAGLKHLNYLENVLAKREARDRGADEALFLDtDGR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 177 VTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKVNDi 256
Cdd:cd01559  155 VIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD- 233

                        250
                 ....*....|....*...
gi 488677036 257 iiGNGARGEITKKIQMLY 274
Cdd:cd01559  234 --HDGPPGPLTRALRELL 249
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 7-279 9.01e-39

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 137.41  E-value: 9.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   7 GSFVDKEDIHIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQNHIENGY 86
Cdd:PRK07650   6 GQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNGLENAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  87 IYLQVTRGDGTLrnhGFS--MYEEqqPVFCGFAQSSTrsEEKMVKGADAITVEDRRslmcN-------VKSLNLLPNCLA 157
Cdd:PRK07650  86 VRFNVSAGIGEI---GLQteMYEE--PTVIVYMKPLA--PPGLPAEKEGVVLKQRR----NtpegafrLKSHHYLNNILG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 158 K----HAAQKKGVskaIMVRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELL 233
Cdd:PRK07650 155 KreigNDPNKEGI---FLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELL 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488677036 234 HADEVMVTDTNSEIVPVIKVNDIIIGnGARGEITKKIQMLYKSLIE 279
Cdd:PRK07650 232 SADEVFVTNSIQEIVPLTRIEERDFP-GKVGMVTKRLQNLYEMQRE 276
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 38-274 2.76e-35

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: 128.08  E-value: 2.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  38 NGVLFALDEHIDRLINSAAFIELNlRHTKDEIAAFCRGLVEQN----HIENG---YIYLQVTRGDGTLrnhgfSMYEEQQ 110
Cdd:cd01557   28 KIVLFRPDENAERLNRSARRLGLP-PFSVEEFIDAIKELVKLDadwvPYGGGaslYIRPFIFGTDPQL-----GVSPALE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 111 PVFCGFAQSSTRSEEKMVKGADAITVEDRR---SLMCNVK-SLNLLPNCLAKHAAQKKGVSKAIMV--RDNIVTEEKSGN 184
Cdd:cd01557  102 YLFAVFASPVGAYFKGGEKGVSALVSSFRRaapGGPGAAKaGGNYAASLLAQKEAAEKGYDQALWLdgAHGYVAEVGTMN 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 185 IFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPV--IKVNDIIIGNGA 262
Cdd:cd01557  182 IFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFATGTAAVVTPVgeIDYRGKEPGEGE 261

                        250
                 ....*....|..
gi 488677036 263 RGEITKKIQMLY 274
Cdd:cd01557  262 VGPVTKKLYDLL 273
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 3-281 2.64e-30

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 115.07  E-value: 2.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   3 YLW-KGSFVDKED--IHIDLHdrGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCRGLVEQ 79
Cdd:PRK07544  10 FIWmDGELVPWRDakVHVLTH--GLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  80 NHIENGYIYLQVTRGDGTLrnhGFSmyEEQQPVFCGFAQ----SSTRSEEKMvKGADAITVEDRR----SLMCNVKSLNL 151
Cdd:PRK07544  88 NGLTDAYVRPVAWRGSEMM---GVS--AQQNKIHLAIAAwewpSYFDPEAKM-KGIRLDIAKWRRpdpeTAPSAAKAAGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 152 LPNC-LAKHAAQKKGVSKAIMV--RDNiVTEEKSGNIFIVKDGIVLThPNGGKILPGITKQLIIELLHQHNIPVWEKEFS 228
Cdd:PRK07544 162 YMICtISKHAAEAKGYADALMLdyRGY-VAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIELAKRRGIEVVERHIM 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488677036 229 EEELLHADEVMVTDTNSEIVPVIKVNDIiigNGARGEITKKIQMLYKSLIEEK 281
Cdd:PRK07544 240 PEELAGFSECFLTGTAAEVTPVSEIGEY---RFTPGAITRDLMDDYEALVRPR 289
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 17-255 4.11e-24

aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 132501  Cd Length: 261  Bit Score: 98.04  E-value: 4.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   17 IDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAA---FIELNLRHTKDEIAAFCRGlveqnhIENGYIYLQVTR 93
Cdd:TIGR03461  10 ISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAArlgIPLPDWDALREEMAQLAAG------YSLGVLKVIISR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036   94 GDGtlrNHGFSMYEEQQP-----VFcGFAQSSTRSEEKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQKKGVSK 168
Cdd:TIGR03461  84 GSG---GRGYSPPGCSDPtriisVS-PYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  169 AIMV-RDNIVTEEKSGNIFIVKDGIVLThpnggkilP--------GITKQLIIELLHQHNIPVWEKEFSEEELLHADEVM 239
Cdd:TIGR03461 160 ALVLdTDGNVVECTAANIFWRKGNQVFT--------PdlsycgvaGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVF 231

                         250
                  ....*....|....*.
gi 488677036  240 VTDTNSEIVPVIKVND 255
Cdd:TIGR03461 232 ITNSLMGVVPVNAIGE 247
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 17-280 8.76e-23

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 95.85  E-value: 8.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  17 IDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNL---RHTKDEI------AAFCRglveqnhieNGYI 87
Cdd:PLN02845  57 IPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLpfdRATLRRIllqtvaASGCR---------NGSL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  88 YLQVTRGDGtlrnhGFSMYEEQ--QPVFCGFAQSSTrSEEKMVKGADAITVED--RRSLMCNVKSLNLLPNCLAKHAAQK 163
Cdd:PLN02845 128 RYWLSAGPG-----GFSLSPSGcsEPAFYAVVIEDT-YAQDRPEGVKVVTSSVpiKPPQFATVKSVNYLPNALSQMEAEE 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 164 KGVSKAIMVRDN-IVTEEKSGNI-FIVKDGIVLTHPNgGKILPGITKQLIIEL---LHQHNI--PVWEKEFSEEELLHAD 236
Cdd:PLN02845 202 RGAFAGIWLDEEgFVAEGPNMNVaFLTNDGELVLPPF-DKILSGCTARRVLELaprLVSPGDlrGVKQRKISVEEAKAAD 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 488677036 237 EVMVTDTNSEIVPVIKVNDIIIGNGARGEITkkiQMLYKSLIEE 280
Cdd:PLN02845 281 EMMLIGSGVPVLPIVSWDGQPIGDGKVGPIT---LALHDLLLDD 321
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 16-256 1.60e-22

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 93.75  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  16 HIDLHDRGYQFGDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELNLRHTK---DEIAAFCRGLveqnhiENGYIYLQVT 92
Cdd:PRK06092  11 SLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAqleQEMKQLAAEL------ENGVLKVIIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  93 RGDGtLRnhGFSMYEEQQP--VFCGFAQSSTRSE--EKMVKGADAITVEDRRSLMCNVKSLNLLPNCLAKHAAQKKGVSK 168
Cdd:PRK06092  85 RGSG-GR--GYSPAGCAAPtrILSVSPYPAHYSRwrEQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEADE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 169 AIMvRD--NIVTEEKSGNIFIVKDGIVLThPN----GgkiLPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVtd 242
Cdd:PRK06092 162 ALV-LDseGWVIECCAANLFWRKGGVVYT-PDldqcG---VAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFI-- 234

                        250
                 ....*....|....
gi 488677036 243 TNSeIVPVIKVNDI 256
Cdd:PRK06092 235 CNS-LMPVWPVRAI 247
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
37-274 1.66e-19

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 85.78  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  37 YNGVLFALDEHIDRLINSAAFIELNLRHTKDEIAAFCR-GLVEQNHIENGYIYlqvtrgdgtlrnhgfSMY--EEQQPVF 113
Cdd:PRK13356  43 FEGVTPDLDLHCARVNRSAEALGLKPTVSAEEIEALAReGLKRFDPDTALYIR---------------PMYwaEDGFASG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 114 CGFAQSSTR-----SEEKMVKGAD-AITVEDRR-----SLMCNVKSLNLLPN-CLAKHAAQKKGVSKAIMvRDNI--VTE 179
Cdd:PRK13356 108 VAPDPESTRfalclEEAPMPEPTGfSLTLSPFRrptleMAPTDAKAGCLYPNnARALREARSRGFDNALV-LDMLgnVAE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 180 EKSGNIFIVKDGIVLTH-PNgGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKVNDIII 258
Cdd:PRK13356 187 TATSNVFMVKDGVVFTPvPN-GTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL 265

                        250
                 ....*....|....*.
gi 488677036 259 gngARGEITKKIQMLY 274
Cdd:PRK13356 266 ---QPGPVTRRARELY 278
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 157-277 6.31e-13

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 68.34  E-value: 6.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 157 AKHAAQKKGVSKAIM---VRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELL 233
Cdd:PLN02782 260 AQSIAKAKGYSDVLYldcVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELL 339

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488677036 234 HADEVMVTDTNSEIVPV----IKVNDIIIGNGARGEITKKiqmLYKSL 277
Cdd:PLN02782 340 EADEVFCTGTAVVVSPVgsitYKGKRVSYGEGGFGTVSQQ---LYTVL 384
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
 156-277 1.06e-11

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 64.40  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 156 LAKHAAQKKGVSKAIMV----RDNIvtEEKSG-NIF-IVKDGIVLThPNGGKILPGITKQLIIELLHQHNIPVWEKEFSE 229
Cdd:PRK13357 206 LAQAEAKEKGCDQVLYLdaveHTYI--EEVGGmNFFfITKDGTVTP-PLSGSILPGITRDSLLQLAEDLGLTVEERPVSI 282

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488677036 230 EELLHA------DEVMVTDTNSEIVPVIKV----NDIIIGNGARGEITKKiqmLYKSL 277
Cdd:PRK13357 283 DEWQADaasgefTEAFACGTAAVITPIGGIkykdKEFVIGDGEVGPVTQK---LYDEL 337
PRK07849 PRK07849
aminodeoxychorismate lyase;
27-255 1.73e-11

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 63.44  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  27 GDGIYEVTHVYNGVLFALDEHIDRLINSAAFIELN------LRH-TKDEIAAFCRglveqnHIENGYIYLQVTRG-DGTL 98
Cdd:PRK07849  38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPepdldrWRRaVELAIEEWRA------PEDEAALRLVYSRGrESGG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036  99 RNHGFSMYeeqQPVfcgfaqsSTRSEEKMVKGADAITVE-------DRRS--LMCNVKSLNLLPNCLAKHAAQKKGVSKA 169
Cdd:PRK07849 112 APTAWVTV---SPV-------PERVARARREGVSVITLDrgypsdaAERApwLLAGAKTLSYAVNMAALRYAARRGADDV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 170 IMVR-DNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIV 248
Cdd:PRK07849 182 IFTStDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAA 261


                 ....*..
gi 488677036 249 PVIKVND 255
Cdd:PRK07849 262 RVHTLDG 268
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 177-253 4.17e-11

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 62.64  E-value: 4.17e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488677036 177 VTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADEVMVTDTNSEIVPVIKV 253
Cdd:PLN03117 232 IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETV 308
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 146-285 1.38e-08

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 55.11  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 146 VKSL-NLLPNCLAKHAAQKKGVSKAIM---VRDNIVTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIP 221
Cdd:PLN02259 234 VKSItNYAPVLKALSRAKSRGFSDVLYldsVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQ 313

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488677036 222 VWEKEFSEEELLHADEVMVTDTNSEIVPVikvndiiigngarGEIT---KKIQmlYKSLIEEKCGKL 285
Cdd:PLN02259 314 VVEKAVHVDEVMDADEVFCTGTAVVVAPV-------------GTITyqeKRVE--YKTGDESVCQKL 365
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 161-250 3.99e-06

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 47.79  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488677036 161 AQKKGVSKAIMVRDNI---VTEEKSGNIFIVKDGIVLTHPNGGKILPGITKQLIIELLHQHNIPVWEKEFSEEELLHADE 237
Cdd:PLN02883 246 AKSRGFSDVLYLDADTgknIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEE 325

                         90
                 ....*....|...
gi 488677036 238 VMVTDTNSEIVPV 250
Cdd:PLN02883 326 VFCTGTAAGVASV 338
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH