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Conserved domains on  [gi|758898745|ref|WP_043054496|]
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MULTISPECIES: DegT/DnrJ/EryC1/StrS aminotransferase family protein [Bacillus]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

CATH:  3.40.640.10|3.90.1150.10
EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
70-436 7.55e-132

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 384.04  E-value: 7.55e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  70 FMPLHR-LITEEEVDdvihAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMP 148
Cdd:COG0399    1 MIPLSRpSIGEEEIA----AVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 149 ANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSI 228
Cdd:COG0399   77 AFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 229 GVSDLGKNS----LCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFElnqknkKAADY-----GFNAKIDNL 299
Cdd:COG0399  157 GATYKGKKVgtfgDAGCFSFYPTKNL-TTGEGGAVVTNDEELAERARSLRNHGRD------RDAKYehvelGYNYRMDEL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 300 QAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDrglIQLPQMTDD--HVWHLFTIKMISG-NRDQVKDMMLKfHNVQT 376
Cdd:COG0399  230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPG---LTLPKVPPGaeHVYHLYVIRLDEGeDRDELIAALKA-RGIGT 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 377 DIYYPILSHHQnTPLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDVV 436
Cdd:COG0399  306 RVHYPIPLHLQ-PAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
70-436 7.55e-132

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 384.04  E-value: 7.55e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  70 FMPLHR-LITEEEVDdvihAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMP 148
Cdd:COG0399    1 MIPLSRpSIGEEEIA----AVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 149 ANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSI 228
Cdd:COG0399   77 AFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 229 GVSDLGKNS----LCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFElnqknkKAADY-----GFNAKIDNL 299
Cdd:COG0399  157 GATYKGKKVgtfgDAGCFSFYPTKNL-TTGEGGAVVTNDEELAERARSLRNHGRD------RDAKYehvelGYNYRMDEL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 300 QAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDrglIQLPQMTDD--HVWHLFTIKMISG-NRDQVKDMMLKfHNVQT 376
Cdd:COG0399  230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPG---LTLPKVPPGaeHVYHLYVIRLDEGeDRDELIAALKA-RGIGT 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 377 DIYYPILSHHQnTPLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDVV 436
Cdd:COG0399  306 RVHYPIPLHLQ-PAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 77-432 3.95e-129

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: 377.01  E-value: 3.95e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   77 ITEEEVDdvihAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATE 156
Cdd:pfam01041   3 IDEEELA----AVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  157 NAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSDLGKN 236
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  237 ----SLCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFELNQKNKKAADY-GFNAKIDNLQAAIGLARMKHL 311
Cdd:pfam01041 159 vgtlGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHEVlGYNYRMTEIQAAIGLAQLERL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  312 SLNNLKRLYLADRYITHLQQYEDRGLIQLPQMTDDHVWHLFTIKMISG--NRDQVKDmMLKFHNVQTDIYYPILSHHQNT 389
Cdd:pfam01041 238 DEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEaiNRDELVE-ALKEAGIGTRVHYPIPLHLQPY 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 758898745  390 PLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEAL 432
Cdd:pfam01041 317 YRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 88-432 2.14e-126

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: 369.95  E-value: 2.14e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  88 AVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATENAVLAAGGTPV 167
Cdd:cd00616    4 AVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 168 FCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSDLGKN----SLCSILS 243
Cdd:cd00616   84 FVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKvgtfGDAGAFS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 244 FNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFELNQKNKKAADYGFNAKIDNLQAAIGLARMKHLSLNNLKRLYLAD 323
Cdd:cd00616  164 FHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 324 RYITHLQQYEDRGLIQLPQMTdDHVWHLFTIKMISGNRDQVKDMM--LKFHNVQTDIYYPILSHHQNTPLVKAdYQHISL 401
Cdd:cd00616  243 RYKELLADLPGIRLPDVPPGV-KHSYHLYVIRLDPEAGESRDELIeaLKEAGIETRVHYPPLHHQPPYKKLLG-YPPGDL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 758898745 402 PVTESVHKQMLQLPLYPGLTVEEQDKVMEAL 432
Cdd:cd00616  321 PNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 77-435 2.30e-75

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: 239.92  E-value: 2.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   77 ITEEEVDDVIHAVKGvlptGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATE 156
Cdd:TIGR03588   8 IDQDDIDAVVEVLKS----DFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  157 NAVLAAGGTPVFCDIDPVTFCMDPSELEACITL----KTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSD 232
Cdd:TIGR03588  84 NCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  233 LGKN------SLCSILSFNPYKNLgTCGKAGAIVTDDPSFAsacmEYMY----HG-----FELNQKNKKAADY-----GF 292
Cdd:TIGR03588 164 GGKPvgncryADATVFSFHPVKII-TTAEGGAVTTNDEELA----ERMRllrsHGitkdpLLFEKQDEGPWYYeqqelGF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  293 NAKIDNLQAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDRGLIQLPQmTDDHVWHLFTIKM---ISGNRDQVKDMML 369
Cdd:TIGR03588 239 NYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPL-GSKSAWHLYPILLdqeFGCTRKEVFEALR 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745  370 KfHNVQTDIYY-PIlsHHQntPLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDV 435
Cdd:TIGR03588 318 A-AGIGVQVHYiPV--HLQ--PYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
69-437 1.17e-65

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 214.89  E-value: 1.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  69 DFMPLHR-LITEEEvddvIHAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIM 147
Cdd:PRK11658   3 DFLPFSRpAMGDEE----LAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 148 PANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQS 227
Cdd:PRK11658  79 PSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 228 IGVSDLGK---NSLCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGF------ELNQKNKKAADY---GFNAK 295
Cdd:PRK11658 159 VGTYYKGRhigARGTAIFSFHAIKNI-TCAEGGLVVTDDDELADRLRSLKFHGLgvdafdRQTQGRAPQAEVltpGYKYN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 296 IDNLQAAIGLARMKHLSLNNLKRLYLADRYithLQQYEDRGL--IQLPQMTDDHVWHLFTIKM---ISG-NRDQvkdMM- 368
Cdd:PRK11658 238 LADINAAIALVQLAKLEALNARRREIAARY---LQALADLPFqpLSLPAWPHQHAWHLFIIRVdeeRCGiSRDA---LMe 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 369 -LKFHNVQTDIYYpILSHHQNtpLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDVVS 437
Cdd:PRK11658 312 aLKERGIGTGLHF-RAAHTQK--YYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAG 378
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
70-436 7.55e-132

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 384.04  E-value: 7.55e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  70 FMPLHR-LITEEEVDdvihAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMP 148
Cdd:COG0399    1 MIPLSRpSIGEEEIA----AVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 149 ANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSI 228
Cdd:COG0399   77 AFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 229 GVSDLGKNS----LCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFElnqknkKAADY-----GFNAKIDNL 299
Cdd:COG0399  157 GATYKGKKVgtfgDAGCFSFYPTKNL-TTGEGGAVVTNDEELAERARSLRNHGRD------RDAKYehvelGYNYRMDEL 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 300 QAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDrglIQLPQMTDD--HVWHLFTIKMISG-NRDQVKDMMLKfHNVQT 376
Cdd:COG0399  230 QAAIGLAQLKRLDEFIARRRAIAARYREALADLPG---LTLPKVPPGaeHVYHLYVIRLDEGeDRDELIAALKA-RGIGT 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 377 DIYYPILSHHQnTPLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDVV 436
Cdd:COG0399  306 RVHYPIPLHLQ-PAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 77-432 3.95e-129

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: 377.01  E-value: 3.95e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   77 ITEEEVDdvihAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATE 156
Cdd:pfam01041   3 IDEEELA----AVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  157 NAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSDLGKN 236
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  237 ----SLCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFELNQKNKKAADY-GFNAKIDNLQAAIGLARMKHL 311
Cdd:pfam01041 159 vgtlGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHEVlGYNYRMTEIQAAIGLAQLERL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  312 SLNNLKRLYLADRYITHLQQYEDRGLIQLPQMTDDHVWHLFTIKMISG--NRDQVKDmMLKFHNVQTDIYYPILSHHQNT 389
Cdd:pfam01041 238 DEFIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEaiNRDELVE-ALKEAGIGTRVHYPIPLHLQPY 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 758898745  390 PLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEAL 432
Cdd:pfam01041 317 YRDLFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 88-432 2.14e-126

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: 369.95  E-value: 2.14e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  88 AVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATENAVLAAGGTPV 167
Cdd:cd00616    4 AVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 168 FCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSDLGKN----SLCSILS 243
Cdd:cd00616   84 FVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKvgtfGDAGAFS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 244 FNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGFELNQKNKKAADYGFNAKIDNLQAAIGLARMKHLSLNNLKRLYLAD 323
Cdd:cd00616  164 FHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 324 RYITHLQQYEDRGLIQLPQMTdDHVWHLFTIKMISGNRDQVKDMM--LKFHNVQTDIYYPILSHHQNTPLVKAdYQHISL 401
Cdd:cd00616  243 RYKELLADLPGIRLPDVPPGV-KHSYHLYVIRLDPEAGESRDELIeaLKEAGIETRVHYPPLHHQPPYKKLLG-YPPGDL 320

                        330       340       350
                 ....*....|....*....|....*....|.
gi 758898745 402 PVTESVHKQMLQLPLYPGLTVEEQDKVMEAL 432
Cdd:cd00616  321 PNAEDLAERVLSLPLHPSLTEEEIDRVIEAL 351
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 77-435 2.30e-75

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: 239.92  E-value: 2.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   77 ITEEEVDDVIHAVKGvlptGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATE 156
Cdd:TIGR03588   8 IDQDDIDAVVEVLKS----DFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  157 NAVLAAGGTPVFCDIDPVTFCMDPSELEACITL----KTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSD 232
Cdd:TIGR03588  84 NCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  233 LGKN------SLCSILSFNPYKNLgTCGKAGAIVTDDPSFAsacmEYMY----HG-----FELNQKNKKAADY-----GF 292
Cdd:TIGR03588 164 GGKPvgncryADATVFSFHPVKII-TTAEGGAVTTNDEELA----ERMRllrsHGitkdpLLFEKQDEGPWYYeqqelGF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  293 NAKIDNLQAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDRGLIQLPQmTDDHVWHLFTIKM---ISGNRDQVKDMML 369
Cdd:TIGR03588 239 NYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPL-GSKSAWHLYPILLdqeFGCTRKEVFEALR 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745  370 KfHNVQTDIYY-PIlsHHQntPLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDV 435
Cdd:TIGR03588 318 A-AGIGVQVHYiPV--HLQ--PYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
69-437 1.17e-65

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 214.89  E-value: 1.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  69 DFMPLHR-LITEEEvddvIHAVKGVLPTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAGIGQGDEVIM 147
Cdd:PRK11658   3 DFLPFSRpAMGDEE----LAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 148 PANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQS 227
Cdd:PRK11658  79 PSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 228 IGVSDLGK---NSLCSILSFNPYKNLgTCGKAGAIVTDDPSFASACMEYMYHGF------ELNQKNKKAADY---GFNAK 295
Cdd:PRK11658 159 VGTYYKGRhigARGTAIFSFHAIKNI-TCAEGGLVVTDDDELADRLRSLKFHGLgvdafdRQTQGRAPQAEVltpGYKYN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 296 IDNLQAAIGLARMKHLSLNNLKRLYLADRYithLQQYEDRGL--IQLPQMTDDHVWHLFTIKM---ISG-NRDQvkdMM- 368
Cdd:PRK11658 238 LADINAAIALVQLAKLEALNARRREIAARY---LQALADLPFqpLSLPAWPHQHAWHLFIIRVdeeRCGiSRDA---LMe 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 369 -LKFHNVQTDIYYpILSHHQNtpLVKADYQHISLPVTESVHKQMLQLPLYPGLTVEEQDKVMEALIDVVS 437
Cdd:PRK11658 312 aLKERGIGTGLHF-RAAHTQK--YYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAG 378
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 118-437 1.54e-53

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 183.11  E-value: 1.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 118 KHVMASSSGTDAMIVALKAAGIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPV 197
Cdd:PRK11706  47 AKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 198 HLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVSDLGKnSLCSI-----LSFNPYKNLgTCGKAGAIVTDDPSFAS-Acm 271
Cdd:PRK11706 127 HYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGR-ALGTIghigcFSFHETKNY-TAGEGGALLINDPALIErA-- 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 272 EYmyhgfeLNQKNKKAADYgFNAKID--------------NLQAAIGLARMKHLSLNNLKRLYLADRYITHLQQYEDRGL 337
Cdd:PRK11706 203 EI------IREKGTNRSQF-FRGQVDkytwvdigssylpsELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGR 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 338 IQLPQMTDD--HVWHLFTIKMISG-NRDQVKDMMlKFHNVQTDIYYPILshHQNTPLVKADYQHISLPVTESVHKQMLQL 414
Cdd:PRK11706 276 IELPSIPDDckHNAHMFYIKLRDLeDRSALINFL-KEAGIMAVFHYIPL--HSSPAGERFGRFHGEDRYTTKESERLLRL 352

                        330       340
                 ....*....|....*....|...
gi 758898745 415 PLYPGLTVEEQDKVMEALIDVVS 437
Cdd:PRK11706 353 PLFYNLTDVEQRTVIDTILEFFS 375
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 75-437 1.58e-31

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 125.00  E-value: 1.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  75 RLITEEEVddvIHAVKGVLpTGQFTSGSYVGVFEAEIAALLRKKHVMASSSGTDAMIVALKA--------AGIGQGDEVI 146
Cdd:PRK15407  40 KVIDAKEL---QNLVDASL-DFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAltspklgdRALKPGDEVI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 147 MPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCILPVHLYGKLPDMEGIAKIADKYGIPIIEDACQ 226
Cdd:PRK15407 116 TVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCD 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 227 SIGVSDLGKNS----LCSILSFNPYKNLgTCGKAGAIVTDDP-------SF---------ASAC---------------- 270
Cdd:PRK15407 196 ALGSTYDGRMTgtfgDIATLSFYPAHHI-TMGEGGAVFTNDPllkkiieSFrdwgrdcwcAPGCdntcgkrfgwqlgelp 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 271 ----MEYMYHGFelnqknkkaadyGFNAKIDNLQAAIGLARMKHLS------LNNLKRLYladryiTHLQQYEDrGLIqL 340
Cdd:PRK15407 275 fgydHKYTYSHL------------GYNLKITDMQAAIGLAQLEKLPgfiearKANFAYLK------EGLASLED-FLI-L 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 341 PQMTD--DHVWHLF--TIKMISG-NRDQVkdmmLKF---HNVQTDIYYP--ILSHhqntPLVKADYQHI--SLPVTESVH 408
Cdd:PRK15407 335 PEATPnsDPSWFGFpiTVKEDAGfTRVEL----VKYleeNKIGTRLLFAgnLTRQ----PYFKGVKYRVvgELTNTDRIM 406

                        410       420
                 ....*....|....*....|....*....
gi 758898745 409 KQMLQLPLYPGLTVEEQDKVMEALIDVVS 437
Cdd:PRK15407 407 NDTFWIGVYPGLTEEMLDYVIEKIEEFFG 435
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 108-223 3.40e-14

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 73.62  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 108 EAeIAALLRKKH--------VMASSSGTDAMIVALkAAGIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVT-FCM 178
Cdd:PRK05764  75 EA-IAAKLKRDNgldydpsqVIVTTGAKQALYNAF-MALLDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKL 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 758898745 179 DPSELEACITLKTKCIL------PV-HLYGKlPDMEGIAKIADKYGIPIIED 223
Cdd:PRK05764 153 TVEQLEAAITPKTKALIlnspsnPTgAVYSP-EELEAIADVAVEHDIWVLSD 203
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 83-225 1.20e-13

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 72.09  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  83 DDVIHAVKGVLPTGQFTSGSYVGVFE--AEIAALLRKKH--------VMASSSGTDAMIVALKAAgIGQGDEVIMPANSF 152
Cdd:COG0436   46 DHIREAAIEALDDGVTGYTPSAGIPElrEAIAAYYKRRYgvdldpdeILVTNGAKEALALALLAL-LNPGDEVLVPDPGY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 153 AATENAVLAAGGTPVFCDIDPVT-FCMDPSELEACITLKTKCIL------PV-HLYGKlPDMEGIAKIADKYGIPIIEDA 224
Cdd:COG0436  125 PSYRAAVRLAGGKPVPVPLDEENgFLPDPEALEAAITPRTKAIVlnspnnPTgAVYSR-EELEALAELAREHDLLVISDE 203


                 .
gi 758898745 225 C 225
Cdd:COG0436  204 I 204
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 107-262 5.39e-13

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: 66.64  E-value: 5.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 107 FEAEIAALL--RKKHVMASSSGTDAMIVALKAAGiGQGDEVIMPANSFAATENAVLAAGG-----TPVFCDIDPVTFCMD 179
Cdd:cd01494    5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSRYWVAAELAGakpvpVPVDDAGYGGLDVAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 180 PSELEAciTLKTKCI---LPVHLYGKLPDMEGIAKIADKYGIPIIEDACQSIGVS----DLGKNSLCSILSFNPYKNLGT 252
Cdd:cd01494   84 LEELKA--KPNVALIvitPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASpapgVLIPEGGADVVTFSLHKNLGG 161

                        170
                 ....*....|
gi 758898745 253 CGkAGAIVTD 262
Cdd:cd01494  162 EG-GGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 107-225 5.14e-11

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: 63.90  E-value: 5.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 107 FEAEIAALLRKKH--------VMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPV-TFC 177
Cdd:cd00609   41 LREAIAEWLGRRGgvdvppeeIVVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFL 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745 178 MDPSELEACITLKTKCIL------PVhlyGKLPDME---GIAKIADKYGIPIIEDAC 225
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYlnnpnnPT---GAVLSEEeleELAELAKKHGILIISDEA 173
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 104-223 7.15e-10

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: 60.29  E-value: 7.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 104 VGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATEN---AVLAAGGTPV-FCDIDpvtfcmD 179
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRlfeRLLPKLGIEVtFVDPD------D 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 758898745 180 PSELEACITLKTKCIL---PVHLYGKLPDMEGIAKIADKYGIPIIED 223
Cdd:cd00614  115 PEALEAAIKPETKLVYvesPTNPTLKVVDIEAIAELAHEHGALLVVD 161
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
82-264 7.30e-10

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 60.01  E-value: 7.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   82 VDDVIHAVKGVLPTGQFT-SGSYVGV--FEAEIAALLRKKHVMAS--------SSGTDAMIVALKAAGIGQGDEVIMPAN 150
Cdd:pfam00155  16 LPAVAKAEKDALAGGTRNlYGPTDGHpeLREALAKFLGRSPVLKLdreaavvfGSGAGANIEALIFLLANPGDAILVPAP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  151 SFAATENAVLAAGGTPVFCDI-DPVTFCMDPSELEACITLKTKCIL---PVHLYGKLPDMEGIAKIAD---KYGI-PIIE 222
Cdd:pfam00155  96 TYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAALKEKPKVVLhtsPHNPTGTVATLEELEKLLDlakEHNIlLLVD 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 758898745  223 DACQSIGVSDLGKNSLCSILSfnPYKNL---GTCGKA--------GAIVTDDP 264
Cdd:pfam00155 176 EAYAGFVFGSPDAVATRALLA--EGPNLlvvGSFSKAfglagwrvGYILGNAA 226
PRK07682 PRK07682
aminotransferase;
110-223 1.20e-09

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 59.75  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 110 EIAALLRKK-HV--------MASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVfcdidPVT----- 175
Cdd:PRK07682  65 EIAKYLKKRfAVsydpndeiIVTVGASQALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPV-----PVAttlen 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 758898745 176 -FCMDPSELEACITLKTKCIL------PV-HLYGKlPDMEGIAKIADKYGIPIIED 223
Cdd:PRK07682 139 eFKVQPAQIEAAITAKTKAILlcspnnPTgAVLNK-SELEEIAVIVEKHDLIVLSD 193
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
118-223 5.92e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 57.42  E-value: 5.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 118 KHVMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCD-IDPVTFCMDPSELEACITLKTKCIL- 195
Cdd:PRK06348  90 NEIMATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIl 168

                         90       100       110
                 ....*....|....*....|....*....|...
gi 758898745 196 -----PVHLYGKLPDMEGIAKIADKYGIPIIED 223
Cdd:PRK06348 169 nspnnPTGAVFSKETLEEIAKIAIEYDLFIISD 201
PRK08248 PRK08248
homocysteine synthase;
106-223 2.47e-07

homocysteine synthase;


Pssm-ID: 236201 [Multi-domain]  Cd Length: 431  Bit Score: 52.54  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 106 VFEAEIAALLRKKHVMASSSGTDAMIVALKAAGiGQGDEVIMPANSFAATEN---AVLAAGGTPV-FcdIDPVtfcmDPS 181
Cdd:PRK08248  68 VFEKRIAALEGGIGALAVSSGQAAITYSILNIA-SAGDEIVSSSSLYGGTYNlfaHTLPKLGITVkF--VDPS----DPE 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 758898745 182 ELEACITLKTKCILPVHL---YGKLPDMEGIAKIADKYGIPIIED 223
Cdd:PRK08248 141 NFEAAITDKTKALFAETIgnpKGDVLDIEAVAAIAHEHGIPLIVD 185
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
124-248 7.32e-07

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.91  E-value: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 124 SSGTDAM-IVALKAAGIGQGDEVIM-----PANsFAATENAVLAAGGTPVFCDIDPvTFCMDPSELEACITLKTKCILPV 197
Cdd:COG0520   84 RGTTEAInLVAYGLGRLKPGDEILItemehHSN-IVPWQELAERTGAEVRVIPLDE-DGELDLEALEALLTPRTKLVAVT 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 758898745 198 HL---YGKLPDMEGIAKIADKYGIPIIEDACQSIG-----VSDLGknslCSILSFNPYK 248
Cdd:COG0520  162 HVsnvTGTVNPVKEIAALAHAHGALVLVDGAQSVPhlpvdVQALG----CDFYAFSGHK 216
MET17 COG2873
O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid ...
 104-223 1.23e-06

O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 442120 [Multi-domain]  Cd Length: 428  Bit Score: 50.41  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 104 VGVFEAEIAALLRKKHVMASSSGTDAMIVALkAAGIGQGDEVIMPANSFAATEN--AVLAA--GGTPVFCDIDpvtfcmD 179
Cdd:COG2873   65 TDVLEKRIAALEGGVAALATASGQAAITLAI-LNLAEAGDHIVASSSLYGGTYNlfAHTLPrlGIEVRFVDPD------D 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 758898745 180 PSELEACITLKTKCIlpvhlYG--------KLPDMEGIAKIADKYGIPIIED 223
Cdd:COG2873  138 PEAFEAAIDPNTKAI-----FGetignpalDVLDIEAIAEIAHEHGVPLIVD 184
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 179-251 1.73e-06

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 49.77  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 179 DPSELEACITLKTKCILPVHL---YGKLPDMEGIAKIADKYGIPIIEDACQSIG-----VSDLGknslCSILSFNPYKNL 250
Cdd:cd06453  128 DLEALEKLLTERTKLVAVTHVsnvLGTINPVKEIGEIAHEAGVPVLVDGAQSAGhmpvdVQDLG----CDFLAFSGHKML 203


                 .
gi 758898745 251 G 251
Cdd:cd06453  204 G 204
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
104-231 4.99e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 47.98  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  104 VGVFEAEIAALLRKKHVMASSSGTDAMIVALKAAgIGQGDEVIM--PANS-FAATENAVLAAGGTPVFCDIDPvTFCMDP 180
Cdd:pfam01212  34 VNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgePAHIhFDETGGHAELGGVQPRPLDGDE-AGNMDL 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758898745  181 SELEACITLKTKCILP----------VHLYG----KLPDMEGIAKIADKYGIPIIED------ACQSIGVS 231
Cdd:pfam01212 112 EDLEAAIREVGADIFPptglislentHNSAGgqvvSLENLREIAALAREHGIPVHLDgarfanAAVALGVI 182
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 105-223 6.90e-06

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 48.17  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 105 GVFEAEIAALLRKKHVMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATEN----AVLAAGGTPVFCDIDpvtfcmDP 180
Cdd:PRK05994  66 AVLEERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINqfghAFKSFGWQVRWADAD------DP 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 758898745 181 SELEACITLKTKCILPVHLY---GKLPDMEGIAKIADKYGIPIIED 223
Cdd:PRK05994 139 ASFERAITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
129-195 1.30e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 47.11  E-value: 1.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745 129 AMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCIL 195
Cdd:PRK06836 108 ALNVALKAI-LNPGDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVI 173
PRK06107 PRK06107
aspartate transaminase;
120-195 1.99e-05

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 46.65  E-value: 1.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745 120 VMASSSGTDAMIVALkAAGIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVT-FCMDPSELEACITLKTKCIL 195
Cdd:PRK06107  96 ITVGGGAKQAIFLAL-MATLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLTPEALEAAITPRTRWLI 171
PRK07683 PRK07683
aminotransferase A; Validated
 118-196 2.28e-05

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 46.26  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 118 KHVMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCI-LP 196
Cdd:PRK07683  90 SEIIVTIGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVvLP 168
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 107-268 7.31e-05

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 44.63  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 107 FEAEIAALLRKKHVMASSSGTDAMIVALkAAGIGQGDEVIMPANSFAATENAvlaaGGTPVFCDIDPVTF-----CMDPS 181
Cdd:cd06502   37 LEARAAELFGKEAALFVPSGTAANQLAL-AAHTQPGGSVICHETAHIYTDEA----GAPEFLSGVKLLPVpgengKLTPE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 182 ELEACITL-------KTK--CILPVHLYG---KLPDMEGIAKIADKYGIPI------IEDACQSIGVSDLGKNSLCSILS 243
Cdd:cd06502  112 DLEAAIRPrddihfpPPSlvSLENTTEGGtvyPLDELKAISALAKENGLPLhldgarLANAAAALGVALKTYKSGVDSVS 191

                        170       180
                 ....*....|....*....|....*
gi 758898745 244 FNPYKNLGTCGkaGAIVTDDPSFAS 268
Cdd:cd06502  192 FCLSKGGGAPV--GAVVVGNRDFIA 214
PRK08912 PRK08912
aminotransferase;
120-214 8.15e-05

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 44.58  E-value: 8.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 120 VMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCIL---P 196
Cdd:PRK08912  90 VMVTSGATEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnP 168

                         90
                 ....*....|....*...
gi 758898745 197 VHLYGKLPDMEGIAKIAD 214
Cdd:PRK08912 169 LNPAGKVFPREELALLAE 186
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 123-225 1.14e-04

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 44.12  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 123 SSSGTDAMIVALKAA--------GIGQGD-----EVIMPANSFAATENAVLAAGGTPVFCDIDPVTFcMDPSELEACI-- 187
Cdd:cd06450   63 TSGGSESNLLALLAArdrarkrlKAGGGRgidklVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGR-MDPEALEAAIde 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 758898745 188 ----TLKTKCI---LPVHLYGKLPDMEGIAKIADKYGIPIIEDAC 225
Cdd:cd06450  142 dkaeGLNPIMVvatAGTTDTGAIDPLEEIADLAEKYDLWLHVDAA 186
PRK07337 PRK07337
pyridoxal phosphate-dependent aminotransferase;
100-250 1.23e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180937  Cd Length: 388  Bit Score: 43.89  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 100 SGSYVGVFEAEIAAllRKKHVMASSSGtdAMIVALkAAGIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVT-FCM 178
Cdd:PRK07337  77 AAWYARRFGLDVAP--ERIVVTAGASA--ALLLAC-LALVERGDEVLMPDPSYPCNRHFVAAAEGRPVLVPSGPAErFQL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 179 DPSELEACITLKTKCIL---PVHLYGK--LPD-MEGI-AKIADKYGIPIIEDACQSIGVSDLGKNSLC------SILSFN 245
Cdd:PRK07337 152 TAADVEAAWGERTRGVLlasPSNPTGTsiAPDeLRRIvEAVRARGGFTIVDEIYQGLSYDAAPVSALSlgddviTINSFS 231


                 ....*
gi 758898745 246 PYKNL 250
Cdd:PRK07337 232 KYFNM 236
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 124-344 1.57e-04

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 43.77  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  124 SSGTDAM-IVALKAA-GIGQGDEVIM-----PANSFAAtENAVLAAGGTPVFCDIDPVTFcMDPSELEACITLKTK--CI 194
Cdd:pfam00266  68 SGTTEAInLVALSLGrSLKPGDEIVItemehHANLVPW-QELAKRTGARVRVLPLDEDGL-LDLDELEKLITPKTKlvAI 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  195 LPV-HLYGKLPDMEGIAKIADKYGIPIIEDACQSIG-----VSDLGknslCSILSFNPYKNLGTCG-------------- 254
Cdd:pfam00266 146 THVsNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGhrpidVQKLG----VDFLAFSGHKLYGPTGigvlygrrdllekm 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  255 ---KAGAIVTDDPSFASACMEYMYHGFELNQKNkKAADYGFNAKIDNLQaAIGLARMKhlslnnlkrlyladRYITHLQQ 331
Cdd:pfam00266 222 pplLGGGGMIETVSLQESTFADAPWKFEAGTPN-IAGIIGLGAALEYLS-EIGLEAIE--------------KHEHELAQ 285

                         250
                  ....*....|...
gi 758898745  332 YEDRGLIQLPQMT 344
Cdd:pfam00266 286 YLYERLLSLPGIR 298
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
 102-225 3.11e-04

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 42.73  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 102 SYVG-----VFEAEIAALLRKKHVMASSSGTDAMIVaLKAAGIGQGDevIMPANS-FAATENAVLAAGGTPVFCDID--- 172
Cdd:cd00617   48 AYAGsksfyDLEDAVQDLFGFKHIIPTHQGRGAENI-LFSILLKPGR--TVPSNMhFDTTRGHIEANGAVPVDLVIDeah 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758898745 173 ------PVTFCMDPSELEA---------------CITLKTKCILPVhlygKLPDMEGIAKIADKYGIPIIEDAC 225
Cdd:cd00617  125 daqeliPFKGNIDVAKLEKlidevgaenipyivlTITNNTAGGQPV----SMANLREVRELAHKYGIPVVLDAA 194
PRK08363 PRK08363
alanine aminotransferase; Validated
 122-223 6.63e-04

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 41.72  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 122 ASSSGTDAMIVALkaagIGQGDEVIMPANSFAATENAVLAAGGTPVFCD-IDPVTFCMDPSELEACITLKTKCIL---PV 197
Cdd:PRK08363 101 AVTEALQLIFGAL----LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAvinPN 176

                         90       100
                 ....*....|....*....|....*....
gi 758898745 198 HLYGKLPD---MEGIAKIADKYGIPIIED 223
Cdd:PRK08363 177 NPTGALYEkktLKEILDIAGEHDLPVISD 205
PLN00175 PLN00175
aminotransferase family protein; Provisional
 97-213 1.54e-03

aminotransferase family protein; Provisional


Pssm-ID: 215089 [Multi-domain]  Cd Length: 413  Bit Score: 40.62  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  97 QFTSGSYVGVFEAEIAALLRK---------KHVMASSSGTDAmIVALKAAGIGQGDEVIMPANSFAATENAVLAAGGTPV 167
Cdd:PLN00175  86 QYARGFGVPELNSAIAERFKKdtglvvdpeKEVTVTSGCTEA-IAATILGLINPGDEVILFAPFYDSYEATLSMAGAKIK 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 758898745 168 FCDIDPVTFCMDPSELEACITLKTKCIL---PVHLYGKLPDMEGIAKIA 213
Cdd:PLN00175 165 TVTLRPPDFAVPEDELKAAFTSKTRAILintPHNPTGKMFTREELELIA 213
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 123-223 2.86e-03

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 39.54  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 123 SSSGTDAMIVALkaagIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFC-----MDPSELEACITLKTK----- 192
Cdd:cd00615   84 TSSSNKAVILAV----CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggIPPETFKKALIEHPDakaav 159

                         90       100       110
                 ....*....|....*....|....*....|.
gi 758898745 193 CILPVHlYGKLPDMEGIAKIADKYGIPIIED 223
Cdd:cd00615  160 ITNPTY-YGICYNLRKIVEEAHHRGLPVLVD 189
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
127-223 4.08e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 39.32  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 127 TDAMIVALKAAgIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITL---KTKCIL---PVHLY 200
Cdd:PRK07309 101 TEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEqgdKLKAVIlnyPANPT 179

                         90       100
                 ....*....|....*....|....*.
gi 758898745 201 GKLPDMEGIAKIAD---KYGIPIIED 223
Cdd:PRK07309 180 GVTYSREQIKALADvlkKYDIFVISD 205
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 106-223 4.11e-03

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 39.24  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 106 VFEAEIAALLRKKHVMASSSGTDAMIVALKAAgIGQGDEVIMPANSFAATE---NAVLAAGGTpvfcDIDPVTFCmDPSE 182
Cdd:PRK07811  65 ALEEQLAALEGGAYGRAFSSGMAATDCLLRAV-LRPGDHIVIPNDAYGGTFrliDKVFTRWGV----EYTPVDLS-DLDA 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 758898745 183 LEACITLKTKCI---LPVHLYGKLPDMEGIAKIADKYGIPIIED 223
Cdd:PRK07811 139 VRAAITPRTKLIwveTPTNPLLSITDIAALAELAHDAGAKVVVD 182
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
 142-230 4.36e-03

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 39.14  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 142 GDEVIMPAN----SFAATENAVLAAGGTPVfcDIDPvTFCMDPSELEACI--TLKTKCILPV--------HLYGKLPDME 207
Cdd:PRK09331 102 GDYVVLDGLahytSYVAAERAGLNVREVPK--TGYP-EYKITPEAYAEKIeeVKEETGKPPAlallthvdGNYGNLADAK 178

                         90       100
                 ....*....|....*....|...
gi 758898745 208 GIAKIADKYGIPIIEDACQSIGV 230
Cdd:PRK09331 179 KVAKVAHEYGIPFLLNGAYTVGR 201
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 141-223 5.30e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 38.71  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745 141 QGDEVIMPANSFAA-TENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCIL---PVHLYGKLPDME---GIAKIA 213
Cdd:PRK08361 116 EGDEVIIPDPAFVCyVEDAKIAEAKPIRIPLREENEFQPDPDELLELITKRTRMIVinyPNNPTGATLDKEvakAIADIA 195

                         90
                 ....*....|
gi 758898745 214 DKYGIPIIED 223
Cdd:PRK08361 196 EDYNIYILSD 205
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 76-223 6.21e-03

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 38.86  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745   76 LITEEEVDDvihAVKGVLPTGQFTS-GSYVGVFEAeiaallRKKHVMASSSGTDAMIVA---LKAAGIGQGDEVIMPANS 151
Cdd:TIGR01265  47 LRTDPEAEE---AVKDALRSGKFNGyAPSVGALAA------REAVAEYLSSDLPGKLTAddvVLTSGCSQAIEICIEALA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758898745  152 fAATENAVLAAGGTP------VFCDIDPVTF-CM-------DPSELEACITLKTKCIL---PVHLYGKLPD---MEGIAK 211
Cdd:TIGR01265 118 -NPGANILVPRPGFPlydtraAFSGLEVRLYdLLpekdweiDLDGLESLADEKTVAIVvinPSNPCGSVFSrdhLQKIAE 196

                         170
                  ....*....|..
gi 758898745  212 IADKYGIPIIED 223
Cdd:TIGR01265 197 VAEKLGIPIIAD 208
PRK12414 PRK12414
putative aminotransferase; Provisional
 120-195 6.78e-03

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 38.62  E-value: 6.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758898745 120 VMASSS-GTDAMIVALkaagIGQGDEVIMPANSFAATENAVLAAGGTPVFCDIDPVTFCMDPSELEACITLKTKCIL 195
Cdd:PRK12414  95 VIASASeGLYAAISAL----VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 200-229 8.02e-03

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 38.14  E-value: 8.02e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 758898745 200 YGKLPDMEGIAKIADKYGIPIIEDACQSIG 229
Cdd:cd06452  152 YGNLHDAKKIAKVCHEYGVPLLLNGAYTVG 181
 
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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