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Conserved domains on  [gi|1678496199|gb|QCX38831|]
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pyridoxal phosphate-dependent aminotransferase [Aureibaculum algae]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
5-353 1.03e-156

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member TIGR04181:

Pssm-ID: 450240  Cd Length: 359  Bit Score: 444.30  E-value: 1.03e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   5 IPLSPSHFSGQEQKYIDKAFAENMISSSyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFT 84
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSV-GAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  85 FSATVNPILYLKATPIFVDSENVTWNMCPHLLE---TSILDRMNK-------GKKPKAIVLVHLYGMPSKMDEIMMISRK 154
Cdd:TIGR04181  80 FVATANAISYLGAEPVFVDVDPDTLGLDPDALEeflEEEAERKDGvlinketGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 155 YNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAP-HYQHSQIGY 233
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPwEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 234 NYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRIRLKDNS 313
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1678496199 314 IESRPLWKPMHLQPVFSDFPNYLNGNSENFFERGLCLPSG 353
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
 
Name Accession Description Interval E-value
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
5-353 1.03e-156

aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.


Pssm-ID: 275034  Cd Length: 359  Bit Score: 444.30  E-value: 1.03e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   5 IPLSPSHFSGQEQKYIDKAFAENMISSSyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFT 84
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSV-GAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  85 FSATVNPILYLKATPIFVDSENVTWNMCPHLLE---TSILDRMNK-------GKKPKAIVLVHLYGMPSKMDEIMMISRK 154
Cdd:TIGR04181  80 FVATANAISYLGAEPVFVDVDPDTLGLDPDALEeflEEEAERKDGvlinketGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 155 YNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAP-HYQHSQIGY 233
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPwEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 234 NYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRIRLKDNS 313
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1678496199 314 IESRPLWKPMHLQPVFSDFPNYLNGNSENFFERGLCLPSG 353
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-371 1.40e-156

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 444.13  E-value: 1.40e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   4 RIPLSPSHFSGQEQKYIDKAFAENMISSsyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTF 83
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL--GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  84 TFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDA 163
Cdd:COG0399    79 TFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAI------TPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 164 AEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAPHYQHSQIGYNYRMTNISAG 243
Cdd:COG0399   153 AQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 244 IGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRIRLKDNSIESRPLW-KP 322
Cdd:COG0399   233 IGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVHYpIP 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678496199 323 MHLQPVFSD--FPNYLNGNSENFFERGLCLPSGSNLTQDNMQEIVDLIKSY 371
Cdd:COG0399   313 LHLQPAYRDlgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
16-369 2.06e-141

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 405.39  E-value: 2.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  16 EQKYIDKAFAENMISSsyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYL 95
Cdd:cd00616     1 ELEAVEEVLDSGWLTL--GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  96 KATPIFVDSENVTWNMCPHLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLK 175
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAI------TPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 176 LGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAPH-YQHSQIGYNYRMTNISAGIGVGQMEMLNL 254
Cdd:cd00616   153 VGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 255 RVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEY--REKLRIRLKDNSIESRPLWKPMHLQPVFSDF 332
Cdd:cd00616   233 IIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGesRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1678496199 333 PNYLNG---NSENFFERGLCLPSGSNLTQDNMQEIVDLIK 369
Cdd:cd00616   313 LGYPPGdlpNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
34-369 7.93e-108

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 320.38  E-value: 7.93e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  34 GSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYLKATPIFVDSENVTWNMCP 113
Cdd:pfam01041  23 GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVFVDIDPDTYNIDP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 114 HLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKII 193
Cdd:pfam01041 103 EAIEAAI------TPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSFHPTKNL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 194 TTSGGGALVSNNSAYCDKALFLATQ--ARDEAPHYQHSQIGYNYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELA 271
Cdd:pfam01041 177 TTGEGGAVVTNDPELAEKARVLRNHgmVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 272 TVKEIYFIDEPQGFFSNRW-LTTLLTD-SFEYREKLRIRLKDNSIESRPL-WKPMHLQPVFSDFPNYLNG---NSENFFE 345
Cdd:pfam01041 257 DLPGFTPLTTPPEADVHAWhLFPILVPeEAINRDELVEALKEAGIGTRVHyPIPLHLQPYYRDLFGYAPGdlpNAEDISS 336
                         330       340
                  ....*....|....*....|....
gi 1678496199 346 RGLCLPSGSNLTQDNMQEIVDLIK 369
Cdd:pfam01041 337 RVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
4-371 8.56e-59

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 194.67  E-value: 8.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   4 RIPLSPSHFSGQEQKYIDKAFAENMISssyGSNitDFeSKICE-----YINVKACTALTSGTAAIHLALILLGIKEGDEV 78
Cdd:PRK11706    1 MIPFNKPPVVGTELDYIQQAMSSGKLC---GDG--GF-TRRCQqwleqRFGSAKVLLTPSCTAALEMAALLLDIQPGDEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  79 ICSTFTFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSILDRMnkgkkpKAIVLVHLYGMPSKMDEIMMISRKYNIP 158
Cdd:PRK11706   75 IMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKT------RAIVPVHYAGVACEMDTIMALAKKHNLF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 159 VIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKA-----------LFLatqaRDEAPHYQ 227
Cdd:PRK11706  149 VVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAeiirekgtnrsQFF----RGQVDKYT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 228 HSQIGYNYRMTNISAGIGVGQMEMLNlRVKARRKNFY-FYKKELATVKE---IYFIDEPQGFFSNRWLTTLLTDSFEYRE 303
Cdd:PRK11706  225 WVDIGSSYLPSELQAAYLWAQLEAAD-RINQRRLALWqRYYDALAPLAEagrIELPSIPDDCKHNAHMFYIKLRDLEDRS 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678496199 304 KLRIRLKDNSIESRPLWKPMHLQPVFSDFpNYLNG---NSENFFERGLCLPSGSNLTQDNMQEIVDLIKSY 371
Cdd:PRK11706  304 ALINFLKEAGIMAVFHYIPLHSSPAGERF-GRFHGedrYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
 
Name Accession Description Interval E-value
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
5-353 1.03e-156

aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.


Pssm-ID: 275034  Cd Length: 359  Bit Score: 444.30  E-value: 1.03e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   5 IPLSPSHFSGQEQKYIDKAFAENMISSSyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFT 84
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSV-GAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  85 FSATVNPILYLKATPIFVDSENVTWNMCPHLLE---TSILDRMNK-------GKKPKAIVLVHLYGMPSKMDEIMMISRK 154
Cdd:TIGR04181  80 FVATANAISYLGAEPVFVDVDPDTLGLDPDALEeflEEEAERKDGvlinketGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 155 YNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAP-HYQHSQIGY 233
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPwEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 234 NYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRIRLKDNS 313
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1678496199 314 IESRPLWKPMHLQPVFSDFPNYLNGNSENFFERGLCLPSG 353
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-371 1.40e-156

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 444.13  E-value: 1.40e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   4 RIPLSPSHFSGQEQKYIDKAFAENMISSsyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTF 83
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL--GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  84 TFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDA 163
Cdd:COG0399    79 TFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAI------TPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 164 AEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAPHYQHSQIGYNYRMTNISAG 243
Cdd:COG0399   153 AQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAKYEHVELGYNYRMDELQAA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 244 IGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRIRLKDNSIESRPLW-KP 322
Cdd:COG0399   233 IGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVHYpIP 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678496199 323 MHLQPVFSD--FPNYLNGNSENFFERGLCLPSGSNLTQDNMQEIVDLIKSY 371
Cdd:COG0399   313 LHLQPAYRDlgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
16-369 2.06e-141

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 405.39  E-value: 2.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  16 EQKYIDKAFAENMISSsyGSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYL 95
Cdd:cd00616     1 ELEAVEEVLDSGWLTL--GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  96 KATPIFVDSENVTWNMCPHLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLK 175
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAI------TPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 176 LGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKALFLATQARDEAPH-YQHSQIGYNYRMTNISAGIGVGQMEMLNL 254
Cdd:cd00616   153 VGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFkYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 255 RVKARRKNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEY--REKLRIRLKDNSIESRPLWKPMHLQPVFSDF 332
Cdd:cd00616   233 IIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGesRDELIEALKEAGIETRVHYPPLHHQPPYKKL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1678496199 333 PNYLNG---NSENFFERGLCLPSGSNLTQDNMQEIVDLIK 369
Cdd:cd00616   313 LGYPPGdlpNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
34-369 7.93e-108

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 320.38  E-value: 7.93e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  34 GSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYLKATPIFVDSENVTWNMCP 113
Cdd:pfam01041  23 GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAKPVFVDIDPDTYNIDP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 114 HLLETSIldrmnkGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKII 193
Cdd:pfam01041 103 EAIEAAI------TPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFSFHPTKNL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 194 TTSGGGALVSNNSAYCDKALFLATQ--ARDEAPHYQHSQIGYNYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELA 271
Cdd:pfam01041 177 TTGEGGAVVTNDPELAEKARVLRNHgmVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 272 TVKEIYFIDEPQGFFSNRW-LTTLLTD-SFEYREKLRIRLKDNSIESRPL-WKPMHLQPVFSDFPNYLNG---NSENFFE 345
Cdd:pfam01041 257 DLPGFTPLTTPPEADVHAWhLFPILVPeEAINRDELVEALKEAGIGTRVHyPIPLHLQPYYRDLFGYAPGdlpNAEDISS 336
                         330       340
                  ....*....|....*....|....
gi 1678496199 346 RGLCLPSGSNLTQDNMQEIVDLIK 369
Cdd:pfam01041 337 RVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
34-370 9.55e-77

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 241.46  E-value: 9.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  34 GSNITDFESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYLKATPIFVDSENVTWNMCP 113
Cdd:TIGR03588  28 GPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 114 HLLETSILDrmNKGKKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLKLGS--LGDIGIFSFNGNK 191
Cdd:TIGR03588 108 DALEKKLAA--AKGKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNcrYADATVFSFHPVK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 192 IITTSGGGALVSNNSAYCDKALFLAT----------QARDEAP-HYQHSQIGYNYRMTNISAGIGVGQMEMLNLRVKARR 260
Cdd:TIGR03588 186 IITTAEGGAVTTNDEELAERMRLLRShgitkdpllfEKQDEGPwYYEQQELGFNYRMTDIQAALGLSQLKKLDRFVAKRR 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 261 KNFYFYKKELATVKEIYFIDEPQGFFSNRWLTTLLTDSFEYREKLRI--RLKDNSIESRPLWKPMHLQPVF------SDF 332
Cdd:TIGR03588 266 EIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVfeALRAAGIGVQVHYIPVHLQPYYrqgfgdGDL 345
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1678496199 333 PnylngNSENFFERGLCLPSGSNLTQDNMQEIVDLIKS 370
Cdd:TIGR03588 346 P-----SAENFYLAEISLPLHPALTLEQQQRVVETLRK 378
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
4-371 8.56e-59

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 194.67  E-value: 8.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   4 RIPLSPSHFSGQEQKYIDKAFAENMISssyGSNitDFeSKICE-----YINVKACTALTSGTAAIHLALILLGIKEGDEV 78
Cdd:PRK11706    1 MIPFNKPPVVGTELDYIQQAMSSGKLC---GDG--GF-TRRCQqwleqRFGSAKVLLTPSCTAALEMAALLLDIQPGDEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  79 ICSTFTFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSILDRMnkgkkpKAIVLVHLYGMPSKMDEIMMISRKYNIP 158
Cdd:PRK11706   75 IMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKT------RAIVPVHYAGVACEMDTIMALAKKHNLF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 159 VIEDAAEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSAYCDKA-----------LFLatqaRDEAPHYQ 227
Cdd:PRK11706  149 VVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAeiirekgtnrsQFF----RGQVDKYT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 228 HSQIGYNYRMTNISAGIGVGQMEMLNlRVKARRKNFY-FYKKELATVKE---IYFIDEPQGFFSNRWLTTLLTDSFEYRE 303
Cdd:PRK11706  225 WVDIGSSYLPSELQAAYLWAQLEAAD-RINQRRLALWqRYYDALAPLAEagrIELPSIPDDCKHNAHMFYIKLRDLEDRS 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678496199 304 KLRIRLKDNSIESRPLWKPMHLQPVFSDFpNYLNG---NSENFFERGLCLPSGSNLTQDNMQEIVDLIKSY 371
Cdd:PRK11706  304 ALINFLKEAGIMAVFHYIPLHSSPAGERF-GRFHGedrYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
18-319 3.04e-48

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 168.91  E-value: 3.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  18 KYIDKAFAENMISSS------YGSNITDFESKICEYINVKACTALTSGTAAIHLAL-----ILLG---IKEGDEVICSTF 83
Cdd:PRK15407   40 KVIDAKELQNLVDASldfwltTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFsaltsPKLGdraLKPGDEVITVAA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  84 TFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSILDrmnkgkKPKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDA 163
Cdd:PRK15407  120 GFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSP------KTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 164 AEAIGSTYKGLKLGSLGDIGIFSFNGNKIITTSGGGALVSNNSaycdkalFLATQA---RD------------------- 221
Cdd:PRK15407  194 CDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDP-------LLKKIIesfRDwgrdcwcapgcdntcgkrf 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 222 -----EAPH-YQH----SQIGYNYRMTNISAGIGVGQMEMLNLRVKARRKNFYFYKKELATVKEIYFIDEPQ-------- 283
Cdd:PRK15407  267 gwqlgELPFgYDHkytySHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPEATpnsdpswf 346
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1678496199 284 GFfsnrwLTTLLTDSFEYREKLRIRLKDNSIESRPL 319
Cdd:PRK15407  347 GF-----PITVKEDAGFTRVELVKYLEENKIGTRLL 377
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
41-261 9.40e-44

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 155.57  E-value: 9.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  41 ESKICEYINVKACTALTSGTAAIHLALILLGIKEGDEVICSTFTFSATVNPILYLKATPIFVDSENVTWNMCPHLLETSI 120
Cdd:PRK11658   39 EQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 121 LDRMnkgkkpKAIVLVHLYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLKLGSLGdIGIFSFNGNKIITTSGGGA 200
Cdd:PRK11658  119 TPRT------KAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGARG-TAIFSFHAIKNITCAEGGL 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678496199 201 LVSNNSAYCDKALFLA------------TQARdeAPHYQHSQIGYNYRMTNISAGIGVGQMEMLNlRVKARRK 261
Cdd:PRK11658  192 VVTDDDELADRLRSLKfhglgvdafdrqTQGR--APQAEVLTPGYKYNLADINAAIALVQLAKLE-ALNARRR 261
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
36-202 3.00e-07

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 49.69  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  36 NITDFESKICEYINVKACTALT--SGTAAIHLALILLGIKeGDEVICST-FTFSATVNPILYLKATPIFVDSENVTWNmc 112
Cdd:cd01494     1 KLEELEEKLARLLQPGNDKAVFvpSGTGANEAALLALLGP-GDEVIVDAnGHGSRYWVAAELAGAKPVPVPVDDAGYG-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199 113 phLLETSILDRMNKGKKPKAIVLVH---LYGMPSKMDEIMMISRKYNIPVIEDAAEAIGSTYKGLKLGSLGDIGIFSFNG 189
Cdd:cd01494    78 --GLDVAILEELKAKPNVALIVITPnttSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSL 155
                         170
                  ....*....|...
gi 1678496199 190 NKIITTSGGGALV 202
Cdd:cd01494   156 HKNLGGEGGGVVI 168
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
5-164 2.52e-06

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 48.88  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199   5 IPLSPSHFSGQEQKYIDKAFAENMISSS---YGSN--ITDFESKICEYINVK---ACTA----LTSG-TAAIHLALILLg 71
Cdd:cd00609     1 IDLSIGEPDFPPPPEVLEALAAAALRAGllgYYPDpgLPELREAIAEWLGRRggvDVPPeeivVTNGaQEALSLLLRAL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678496199  72 IKEGDEVICSTFTFSATVNPILYLKATPIFV--DSENvtwnmcpHLLETSILDRMNKGKKPKAIVLV-------HLYGmP 142
Cdd:cd00609    80 LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVplDEEG-------GFLLDLELLEAAKTPKTKLLYLNnpnnptgAVLS-E 151
                         170       180
                  ....*....|....*....|..
gi 1678496199 143 SKMDEIMMISRKYNIPVIEDAA 164
Cdd:cd00609   152 EELEELAELAKKHGILIISDEA 173
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
36-103 1.46e-03

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 40.26  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678496199  36 NITDFESKICEYINVKACTALTSGTAAIHLALILLgIKEGDEVICS------TFTFSATVNPILYLKATpiFVD 103
Cdd:cd00614    41 TVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASddlyggTYRLFERLLPKLGIEVT--FVD 111
 
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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