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Conserved domains on  [gi|215706429|dbj|BAG93285|]
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unnamed protein product [Oryza sativa Japonica Group]

Protein Classification

aminotransferase class IV; class IV aminotransferase( domain architecture ID 1908164)

aminotransferase class IV is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE), similar to Staphylococcus D-alanine aminotransferase; class IV aminotransferase is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE) and may be a branched-chain amino acid aminotransferase, a D-amino acid transferase, or a 4-amino-4-deoxychorismate lyase; contains a SAM-dependent methyltransferase domain

Graphical summary

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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, ...
 168-378 3.01e-77

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: 240.19  E-value: 3.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 168 WVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNAN-GM 246
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNeGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 FNNAHIRltLTRGKKVTSGMSPAfnlYGCTLIVLAEWKPPVY---DNSHGIKLVTATTRRNspNSIDSKIHhnNLINNIL 323
Cdd:cd01558   81 EGDVYIQ--VTRGVGPRGHDFPK---CVKPTVVIITQPLPLPpaeLLEKGVRVITVPDIRW--LRCDIKSL--NLLNNVL 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215706429 324 AKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHA-EYCLPGITRATV 378
Cdd:cd01558  152 AKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLdNGILPGITRATV 207
Sulfotransfer_5 super family cl45194
Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This ...
 6-138 4.84e-25

Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 238 and 379 amino acids in length.


The actual alignment was detected with superfamily member pfam19798:

Pssm-ID: 437630  Cd Length: 226  Bit Score: 102.02  E-value: 4.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429    6 HFILIRNPLNILPSF----DKVVPPsffELGIAELVSIYSELCELgspppVIDADDLQRDPEAVLSGLCEDLGIPYQPQM 81
Cdd:pfam19798  97 HLHLIRHPARVIASYgakrDDITEA---DIAFAAQATLYDRVGGL-----VVDTADLRDDPAGMLAKLCAEMGIPFDPAM 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429   82 LQWEAGPKDFDGIWAPWWYRSVHKSTGFSMPRRyPLTfPFALYDLLEQSLPFYNVLK 138
Cdd:pfam19798 169 LSWPSGGHAADGIWAAHWYNAVHRSTGFAGPEG-PLP-QVSRDDLLAAAMPFYKAMK 223
 
Name Accession Description Interval E-value
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 168-378 3.01e-77

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: 240.19  E-value: 3.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 168 WVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNAN-GM 246
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNeGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 FNNAHIRltLTRGKKVTSGMSPAfnlYGCTLIVLAEWKPPVY---DNSHGIKLVTATTRRNspNSIDSKIHhnNLINNIL 323
Cdd:cd01558   81 EGDVYIQ--VTRGVGPRGHDFPK---CVKPTVVIITQPLPLPpaeLLEKGVRVITVPDIRW--LRCDIKSL--NLLNNVL 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215706429 324 AKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHA-EYCLPGITRATV 378
Cdd:cd01558  152 AKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLdNGILPGITRATV 207
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 165-378 1.05e-69

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: 221.22  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 165 ILVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNAN 244
Cdd:COG0115    1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 245 GMfNNAHIRLTLTRGkkvTSGMSPAFNLYGCTLIVLA-EWKPPVYDN-SHGIKLVTATTRRNSPNSiDSKIHHNNLINNI 322
Cdd:COG0115   81 GL-EDGYIRPQVTRG---VGGRGVFAEEYEPTVIIIAsPLPAYPAEAyEKGVRVITSPYRRAAPGG-LGGIKTGNYLNNV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429 323 LAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHA-EYCLPGITRATV 378
Cdd:COG0115  156 LAKQEAKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLsGGILPGITRDSV 212
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 165-378 3.77e-65

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 209.73  E-value: 3.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 165 ILVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFsNVP-SRDWIKDAIFRTLNA 243
Cdd:PRK08320   3 QLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIML-EIPlSKEEMTEIVLETLRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 244 NGMfNNAHIRLTLTRGKKvTSGMSPafnlYGC---TLIVLAE-WKP---PVYDNshGIKLVTATTRRNSPNSIDSKIHHN 316
Cdd:PRK08320  82 NNL-RDAYIRLVVSRGVG-DLGLDP----RKCpkpTVVCIAEpIGLypgELYEK--GLKVITVSTRRNRPDALSPQVKSL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215706429 317 NLINNILAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAgALEGITRNAV 216
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 193-378 3.54e-35

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: 129.40  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  193 AVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGMFNnAHIRLTLTRGKKVTSGMSPAFNL 272
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGV-GRLRLTVSRGPGGFGLPTSDPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  273 YgctlIVLAEWKPPVYdnSHGIKLVTATTRRNSPNSiDSKIHHNNLINNILAKIEGNLAQAEDAIMLDKDGFVSETNATN 352
Cdd:pfam01063  80 A----IFVSALPPPPE--SKKKGVISSLVRRNPPSP-LPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSN 152

                         170       180
                  ....*....|....*....|....*..
gi 215706429  353 IFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:pfam01063 153 VFLVKGGTLYTPPLESgILPGITRQAL 179
Sulfotransfer_5 pfam19798
Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This ...
 6-138 4.84e-25

Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 238 and 379 amino acids in length.


Pssm-ID: 437630  Cd Length: 226  Bit Score: 102.02  E-value: 4.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429    6 HFILIRNPLNILPSF----DKVVPPsffELGIAELVSIYSELCELgspppVIDADDLQRDPEAVLSGLCEDLGIPYQPQM 81
Cdd:pfam19798  97 HLHLIRHPARVIASYgakrDDITEA---DIAFAAQATLYDRVGGL-----VVDTADLRDDPAGMLAKLCAEMGIPFDPAM 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429   82 LQWEAGPKDFDGIWAPWWYRSVHKSTGFSMPRRyPLTfPFALYDLLEQSLPFYNVLK 138
Cdd:pfam19798 169 LSWPSGGHAADGIWAAHWYNAVHRSTGFAGPEG-PLP-QVSRDDLLAAAMPFYKAMK 223
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 178-386 2.82e-17

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: 81.09  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  178 SAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVpsrDW-IKDAIFRTLNANGMfnNAHIRLTL 256
Cdd:TIGR03461   7 QTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLP---DWdALREEMAQLAAGYS--LGVLKVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  257 TRGKKvTSGMSPAfnlyGCT----LIVLAEWkPPVYDN--SHGIKLVTATTRRnSPNSIDSKIHHNNLINNILAKIEGNL 330
Cdd:TIGR03461  82 SRGSG-GRGYSPP----GCSdptrIISVSPY-PAHYSAwqQQGIRLGVSPVRL-GRNPLLAGIKHLNRLEQVLIKAELEN 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429  331 AQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATVSLIRFQLE 386
Cdd:TIGR03461 155 SEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCgVAGVMRQHVLALLPALG 211
 
Name Accession Description Interval E-value
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 168-378 3.01e-77

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: 240.19  E-value: 3.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 168 WVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNAN-GM 246
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNeGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 FNNAHIRltLTRGKKVTSGMSPAfnlYGCTLIVLAEWKPPVY---DNSHGIKLVTATTRRNspNSIDSKIHhnNLINNIL 323
Cdd:cd01558   81 EGDVYIQ--VTRGVGPRGHDFPK---CVKPTVVIITQPLPLPpaeLLEKGVRVITVPDIRW--LRCDIKSL--NLLNNVL 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215706429 324 AKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHA-EYCLPGITRATV 378
Cdd:cd01558  152 AKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLdNGILPGITRATV 207
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 165-378 1.05e-69

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: 221.22  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 165 ILVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNAN 244
Cdd:COG0115    1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 245 GMfNNAHIRLTLTRGkkvTSGMSPAFNLYGCTLIVLA-EWKPPVYDN-SHGIKLVTATTRRNSPNSiDSKIHHNNLINNI 322
Cdd:COG0115   81 GL-EDGYIRPQVTRG---VGGRGVFAEEYEPTVIIIAsPLPAYPAEAyEKGVRVITSPYRRAAPGG-LGGIKTGNYLNNV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429 323 LAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHA-EYCLPGITRATV 378
Cdd:COG0115  156 LAKQEAKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLsGGILPGITRDSV 212
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 165-378 3.77e-65

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 209.73  E-value: 3.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 165 ILVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFsNVP-SRDWIKDAIFRTLNA 243
Cdd:PRK08320   3 QLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIML-EIPlSKEEMTEIVLETLRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 244 NGMfNNAHIRLTLTRGKKvTSGMSPafnlYGC---TLIVLAE-WKP---PVYDNshGIKLVTATTRRNSPNSIDSKIHHN 316
Cdd:PRK08320  82 NNL-RDAYIRLVVSRGVG-DLGLDP----RKCpkpTVVCIAEpIGLypgELYEK--GLKVITVSTRRNRPDALSPQVKSL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215706429 317 NLINNILAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAgALEGITRNAV 216
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 185-378 3.93e-56

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: 185.11  E-value: 3.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 185 DSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGmFNNAHIRLTLTRGKKVTS 264
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANN-GASLYIRPLLTRGVGGLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 265 GMSPAFNLYgcTLIVLA-EWKPPVYDNSHGIKLVTATTRRNSPNSIDSKIHHNNLINNILAKIEGNLAQAEDAIMLDKDG 343
Cdd:cd00449   80 VAPPPSPEP--TFVVFAsPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNG 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 215706429 344 FVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATV 378
Cdd:cd00449  158 YVTEGSASNVFIVKDGELVTPPLDGGiLPGITRDSV 193
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
163-378 1.13e-44

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 156.65  E-value: 1.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 163 KKILVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLN 242
Cdd:PRK12479   2 GNQYIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 243 ANGmFNNAHIRLTLTRGKKvTSGMSPAfNLYGCTLIVLAE----WKPPVYDNshGIKLVTATTRRNSPNSIDSKIHHNNL 318
Cdd:PRK12479  82 KNE-YADAYIRLIVSRGKG-DLGLDPR-SCVKPSVIIIAEqlklFPQEFYDN--GLSVVSVASRRNTPDALDPRIKSMNY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215706429 319 INNILAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:PRK12479 157 LNNVLVKIEAAQAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLgALEGITRNSV 217
PRK06606 PRK06606
branched-chain amino acid transaminase;
166-378 9.35e-40

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 143.75  E-value: 9.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 166 LVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGK----VFKLDEHLDRLFDSAKAMAFsNVP-SRDWIKDAIFRT 240
Cdd:PRK06606   8 YIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPkgpaIFRLREHTKRLFNSAKILRM-EIPySVDELMEAQREV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 241 LNANGmFNNAHIRLTLTRGkkvTSGMSPAFNLYGCTLIVlAEWKPPVY----DNSHGIKLVTATTRRNSPNSIDSKIHHN 316
Cdd:PRK06606  87 VRKNN-LKSAYIRPLVFVG---DEGLGVRPHGLPTDVAI-AAWPWGAYlgeeALEKGIRVKVSSWTRHAPNSIPTRAKAS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215706429 317 -NLINNILAKIEGNLAQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTP-HAEYCLPGITRATV 378
Cdd:PRK06606 162 gNYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGENIFIVRDGVLYTPpLTSSILEGITRDTV 225
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 193-378 3.54e-35

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: 129.40  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  193 AVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGMFNnAHIRLTLTRGKKVTSGMSPAFNL 272
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGV-GRLRLTVSRGPGGFGLPTSDPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  273 YgctlIVLAEWKPPVYdnSHGIKLVTATTRRNSPNSiDSKIHHNNLINNILAKIEGNLAQAEDAIMLDKDGFVSETNATN 352
Cdd:pfam01063  80 A----IFVSALPPPPE--SKKKGVISSLVRRNPPSP-LPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSN 152

                         170       180
                  ....*....|....*....|....*..
gi 215706429  353 IFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:pfam01063 153 VFLVKGGTLYTPPLESgILPGITRQAL 179
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 185-378 2.34e-32

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: 122.42  E-value: 2.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 185 DSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNvPSRDWIKDAIFRTLNANGMfNNAHIRLTLTRG---KK 261
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPE-PDLPRLRAALESLLAANDI-DEGRIRLILSRGpggRG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 262 VTSGMSPAFNLYGCTLIVLAEWKPpvydnsHGIKLVTATTRRNSPnSIDSKIHHNNLINNILAKIEGNLAQAEDAIMLDK 341
Cdd:cd01559   79 YAPSVCPGPALYVSVIPLPPAWRQ------DGVRLITCPVRLGEQ-PLLAGLKHLNYLENVLAKREARDRGADEALFLDT 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 215706429 342 DGFVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATV 378
Cdd:cd01559  152 DGRVIEGTASNLFFVKDGELVTPSLDRGgLAGITRQRV 189
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 167-378 3.65e-29

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 115.07  E-value: 3.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 167 VWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGm 246
Cdd:PRK07544  11 IWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANG- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 FNNAHIRLTLTRGKK---VTSGMSPafnlygcTLIVLAEWKPPVY----DNSHGIKLVTATTRRNSPNSIDSKIHHNNLI 319
Cdd:PRK07544  90 LTDAYVRPVAWRGSEmmgVSAQQNK-------IHLAIAAWEWPSYfdpeAKMKGIRLDIAKWRRPDPETAPSAAKAAGLY 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215706429 320 nnILAKIEGNLAQAE---DAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEYCLPGITRATV 378
Cdd:PRK07544 163 --MICTISKHAAEAKgyaDALMLDYRGYVAEATGANIFFVKDGVIHTPTPDCFLDGITRQTV 222
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 166-378 3.26e-26

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 106.59  E-value: 3.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 166 LVWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANG 245
Cdd:PRK07650   1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 246 MfNNAHIRLTLTRGKKvTSGMSPAFNLYGCTLIVLAEWKPPvyDNSHGIKLVTATTRRNSPN-SIDSKIHHnnLINNILA 324
Cdd:PRK07650  81 L-ENAYVRFNVSAGIG-EIGLQTEMYEEPTVIVYMKPLAPP--GLPAEKEGVVLKQRRNTPEgAFRLKSHH--YLNNILG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 215706429 325 KIE-GNLAQAEdAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEY-CLPGITRATV 378
Cdd:PRK07650 155 KREiGNDPNKE-GIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETgILNGITRAFV 209
Sulfotransfer_5 pfam19798
Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This ...
 6-138 4.84e-25

Sulfotransferase domain; This entry represents a family of sulfotransferase enzymes. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 238 and 379 amino acids in length.


Pssm-ID: 437630  Cd Length: 226  Bit Score: 102.02  E-value: 4.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429    6 HFILIRNPLNILPSF----DKVVPPsffELGIAELVSIYSELCELgspppVIDADDLQRDPEAVLSGLCEDLGIPYQPQM 81
Cdd:pfam19798  97 HLHLIRHPARVIASYgakrDDITEA---DIAFAAQATLYDRVGGL-----VVDTADLRDDPAGMLAKLCAEMGIPFDPAM 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429   82 LQWEAGPKDFDGIWAPWWYRSVHKSTGFSMPRRyPLTfPFALYDLLEQSLPFYNVLK 138
Cdd:pfam19798 169 LSWPSGGHAADGIWAAHWYNAVHRSTGFAGPEG-PLP-QVSRDDLLAAAMPFYKAMK 223
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 180-378 2.09e-23

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: 98.81  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 180 KVSVFDSVVQGGDAVWEGLRIYDGK-----VFKLDEHLDRLFDSAKAMAFSNVPSrDWIKDAIFRTLNANGMFN------ 248
Cdd:cd01557    1 SLHPATHALHYGQAVFEGLKAYRTPdgkivLFRPDENAERLNRSARRLGLPPFSV-EEFIDAIKELVKLDADWVpyggga 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 249 NAHIRLTL-TRGKKVTSGMSPAFNLYgctlIVLAEWKPPVYDNSHGIKLVTATTRRNSPNSI-DSKIHhNNLINNILAKI 326
Cdd:cd01557   80 SLYIRPFIfGTDPQLGVSPALEYLFA----VFASPVGAYFKGGEKGVSALVSSFRRAAPGGPgAAKAG-GNYAASLLAQK 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 215706429 327 EGNLAQAEDAIMLD-KDGFVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATV 378
Cdd:cd01557  155 EAAEKGYDQALWLDgAHGYVAEVGTMNIFFVKDGELITPPLDGSiLPGITRDSI 208
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 167-378 2.61e-18

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 84.60  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 167 VWVGDELLPRDSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGm 246
Cdd:PRK06680   5 AYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNR- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 FNNAHIRLTLTRGKKVTSGMSPAFNLYGcTLIVLAEWKPPVYD---NSHGIKLVTATTRRNSPNSIDSKihhnNLINNIL 323
Cdd:PRK06680  84 VREGLVYLQVTRGVARRDHVFPAADVKP-SVVVFAKSVDFARPaaaAETGIKVITVPDNRWKRCDIKSV----GLLPNVL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429 324 AKIEGNLAQAEDAIMLDkDGFVSETNATNIFMVKK-GIVLT-PHAEYCLPGITRATV 378
Cdd:PRK06680 159 AKQAAKEAGAQEAWMVD-DGFVTEGASSNAWIVTKdGKLVTrPADNFILPGITRHTL 214
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 178-386 2.82e-17

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: 81.09  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  178 SAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVpsrDW-IKDAIFRTLNANGMfnNAHIRLTL 256
Cdd:TIGR03461   7 QTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLP---DWdALREEMAQLAAGYS--LGVLKVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429  257 TRGKKvTSGMSPAfnlyGCT----LIVLAEWkPPVYDN--SHGIKLVTATTRRnSPNSIDSKIHHNNLINNILAKIEGNL 330
Cdd:TIGR03461  82 SRGSG-GRGYSPP----GCSdptrIISVSPY-PAHYSAwqQQGIRLGVSPVRL-GRNPLLAGIKHLNRLEQVLIKAELEN 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215706429  331 AQAEDAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATVSLIRFQLE 386
Cdd:TIGR03461 155 SEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCgVAGVMRQHVLALLPALG 211
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 185-381 1.75e-14

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 73.90  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 185 DSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAkAMAFSNVP-SRDWIKDAIFRTLNANGMfNNAHIRLTLTRGkkvt 263
Cdd:PLN02845  61 DHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSA-AKAKIPLPfDRATLRRILLQTVAASGC-RNGSLRYWLSAG---- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 264 SG---MSPAfnlyGC---TLIVLAEWKPPVYDNSHGIKLVTATTRRNSPNSidSKIHHNNLINNILAKIEGNLAQAEDAI 337
Cdd:PLN02845 135 PGgfsLSPS----GCsepAFYAVVIEDTYAQDRPEGVKVVTSSVPIKPPQF--ATVKSVNYLPNALSQMEAEERGAFAGI 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 215706429 338 MLDKDGFVSETNATNI-FMVKKGIVLTPHAEYCLPGIT-RATVSLI 381
Cdd:PLN02845 209 WLDEEGFVAEGPNMNVaFLTNDGELVLPPFDKILSGCTaRRVLELA 254
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 166-364 5.21e-14

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 71.41  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 166 LVWV-GdelLPRDSakVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFsnvPSRDW--IKDAIFRTLN 242
Cdd:PRK06092   1 MFWInG---QPQES--LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAI---PLDDWaqLEQEMKQLAA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 243 ANGmfnNAHIRLTLTRGkkvTS--GMSPAfnlyGC--TLIVLAEWKPPVYDNSH---GIKLVTATTRRnSPNSIDSKIHH 315
Cdd:PRK06092  73 ELE---NGVLKVIISRG---SGgrGYSPA----GCaaPTRILSVSPYPAHYSRWreqGITLALCPTRL-GRNPLLAGIKH 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 215706429 316 NNLINNILAKIEgnLAQAE--DAIMLDKDGFVSETNATNIFMVKKGIVLTP 364
Cdd:PRK06092 142 LNRLEQVLIRAE--LEQTEadEALVLDSEGWVIECCAANLFWRKGGVVYTP 190
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 188-378 2.48e-10

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 60.80  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 188 VQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIFRTLNANGMFNNAHIRLTLTRGKKVTSgMS 267
Cdd:PRK12400  30 LQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFHEDGTIYLQVSRGVQART-HT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 268 PAFNLYGCTLIVLAEWKPPVYDNSHGIKLVTATTRRnspnSIDSKIHHNNLINNILAKIEGNLAQAEDAIMLdKDGFVSE 347
Cdd:PRK12400 109 FSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTR----WLRCDIKSLNLLPNILAATKAERKGCKEALFV-RNGTVTE 183

                        170       180       190
                 ....*....|....*....|....*....|..
gi 215706429 348 TNATNIFMVKKGIVLT-PHAEYCLPGITRATV 378
Cdd:PRK12400 184 GSHSNFFLIKNGTLYThPANHLILNGIIRQYV 215
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
191-382 2.42e-08

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 54.96  E-value: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 191 GDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDWIKDAIF---RTLNANG------MFNNAHirltltrgkk 261
Cdd:PRK13356  33 GSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLKPTVSAEEIEALAReglKRFDPDTalyirpMYWAED---------- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 262 vTSGMSPAFNLyGCTLIVLAEWKPPVyDNSHGIKLVTATTRRNSPNS--IDSK---IHHNN--LINNILAKIEGNlaqae 334
Cdd:PRK13356 103 -GFASGVAPDP-ESTRFALCLEEAPM-PEPTGFSLTLSPFRRPTLEMapTDAKagcLYPNNarALREARSRGFDN----- 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 215706429 335 dAIMLDKDGFVSETNATNIFMVKKGIVLTPHAEYC-LPGITRATV-SLIR 382
Cdd:PRK13356 175 -ALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTfLNGITRQRViALLR 223
PRK07849 PRK07849
aminodeoxychorismate lyase;
165-264 6.41e-08

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 53.81  E-value: 6.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 165 ILVWV-GDELLPR----DSAKVSVFDSVVQGGDAVWEGLRIYDGKVFKLDEHLDRLFDSAKAMAFSNVPSRDW---IKDA 236
Cdd:PRK07849   7 VVVTLdPYGGSERvhdpSAPLLHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEPDLDRWrraVELA 86

                         90       100
                 ....*....|....*....|....*...
gi 215706429 237 IfRTLNANGmfNNAHIRLTLTRGKKVTS 264
Cdd:PRK07849  87 I-EEWRAPE--DEAALRLVYSRGRESGG 111
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 172-379 6.55e-06

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 47.62  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 172 ELLPRDSAKVSVFDSVVQGGDAVWEGLRIY---DGKV--FKLDEHLDRLFDSAKAMAFSnVPSRDWIKDAIFRTLNANGM 246
Cdd:PLN03117  50 KIVPYGDISISPCAGILNYGQGLFEGLKAYrteDGRItlFRPDQNALRMQTGADRLCMT-PPSLEQFVEAVKQTVLANKK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215706429 247 F------NNAHIRLTLTrGKKVTSGMSPA----FNLYGCtlivlaewkpPV---YDNSHGIKL-VTATTRRNSPNSIDSK 312
Cdd:PLN03117 129 WvpppgkGTLYIRPLLI-GSGAVLGVAPApeytFLIYAS----------PVgnyHKASSGLNLkVDHKHRRAHSGGTGGV 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215706429 313 IHHNNLINNILAKIEGNLAQAEDAIMLD----KDgfVSETNATNIFMVKKGIVLTPH-AEYCLPGITRATVS 379
Cdd:PLN03117 198 KSCTNYSPVVKSLIEAKSSGFSDVLFLDaatgKN--IEELSACNIFILKGNIVSTPPtSGTILPGVTRKSIS 267
 
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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