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Conserved domains on  [gi|446150946|ref|WP_000228801|]
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MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase [Leptospira]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10089755)

DegT/DnrJ/EryC1/StrS family aminotransferase belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I), such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

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
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-358 1.89e-130

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: 377.27  E-value: 1.89e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  17 EIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYLLGA 96
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  97 KVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQSDIG 176
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 177 CFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVENVKDPKTWAMPGFNFRFTDILASIGIEQLKILPERIEYLKEI 256
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 257 YQVYLEGLKDLSINCIPvKIETGEVPVY-------TEYLANDREDFIQNLSKAEIDSRPFYPDLDKASYFPQ----GNRD 325
Cdd:cd00616  241 AERYKELLADLPGIRLP-DVPPGVKHSYhlyvirlDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKllgyPPGD 319

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446150946 326 FPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIK 358
Cdd:cd00616  320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
 
Name Accession Description Interval E-value
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-358 1.89e-130

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: 377.27  E-value: 1.89e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  17 EIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYLLGA 96
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  97 KVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQSDIG 176
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 177 CFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVENVKDPKTWAMPGFNFRFTDILASIGIEQLKILPERIEYLKEI 256
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 257 YQVYLEGLKDLSINCIPvKIETGEVPVY-------TEYLANDREDFIQNLSKAEIDSRPFYPDLDKASYFPQ----GNRD 325
Cdd:cd00616  241 AERYKELLADLPGIRLP-DVPPGVKHSYhlyvirlDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKllgyPPGD 319

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446150946 326 FPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIK 358
Cdd:cd00616  320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
10-361 3.04e-120

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 351.68  E-value: 3.04e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:COG0399    6 RPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  90 APYLLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFL 169
Cdd:COG0399   86 AILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 170 GTQSDIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVEnvKDPK-TWAMPGFNFRFTDILASIGIEQLKILPE 248
Cdd:COG0399  166 GTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD--RDAKyEHVELGYNYRMDELQAAIGLAQLKRLDE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 249 RIEYLKEIYQVYLEGLKDLSiNCIPVKIETGEVPVYTEY-----LANDREDFIQNLSKAEIDSRPFYPD-LDKASYF--- 319
Cdd:COG0399  244 FIARRRAIAARYREALADLP-GLTLPKVPPGAEHVYHLYvirldEGEDRDELIAALKARGIGTRVHYPIpLHLQPAYrdl 322

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446150946 320 PQGNRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIKKIY 361
Cdd:COG0399  323 GYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 14-358 3.43e-99

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: 298.04  E-value: 3.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   14 EEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYL 93
Cdd:pfam01041   4 DEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   94 LGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQS 173
Cdd:pfam01041  84 LGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  174 DIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVENVKDPKTWA-MPGFNFRFTDILASIGIEQLKILPERIEY 252
Cdd:pfam01041 164 DAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHeVLGYNYRMTEIQAAIGLAQLERLDEFIAR 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  253 LKEIYQVYLEGLKDLSINCIPVKIETGEV------PVYTEYLANDREDFIQNLSKAEIDSRPFYPDLDK-----ASYFPQ 321
Cdd:pfam01041 244 RREIAALYQTLLADLPGFTPLTTPPEADVhawhlfPILVPEEAINRDELVEALKEAGIGTRVHYPIPLHlqpyyRDLFGY 323

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446150946  322 GNRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIK 358
Cdd:pfam01041 324 APGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 10-360 5.99e-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: 236.46  E-value: 5.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:TIGR03588   5 RQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   90 APYLLGAKVVLVDVESDRPIIDVTKVEEIIT----PRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNN 165
Cdd:TIGR03588  85 CALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  166 RGFLGTQ--SDIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVEnvKDPKTWAMP------------GFNFRF 231
Cdd:TIGR03588 165 GKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGIT--KDPLLFEKQdegpwyyeqqelGFNYRM 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  232 TDILASIGIEQLKILPERIEYLKEIYQVYLEGLKDLSInCIPVKIETGEVPVYTEY-------LANDREDFIQNLSKAEI 304
Cdd:TIGR03588 243 TDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPY-FTPLTIPLGSKSAWHLYpilldqeFGCTRKEVFEALRAAGI 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446150946  305 DSRPFYPDLDKASYFPQG--NRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIKKI 360
Cdd:TIGR03588 322 GVQVHYIPVHLQPYYRQGfgDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
10-267 2.55e-55

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 185.61  E-value: 2.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:PRK11658   9 RPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  90 APYLLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSK-NNR-- 166
Cdd:PRK11658  89 MIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYyKGRhi 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 167 GFLGTqsdiGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVE-NVKDPKTWA--------MPGFNFRFTDILAS 237
Cdd:PRK11658 169 GARGT----AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGvDAFDRQTQGrapqaevlTPGYKYNLADINAA 244

                        250       260       270
                 ....*....|....*....|....*....|
gi 446150946 238 IGIEQLKILPERIEYLKEIYQVYLEGLKDL 267
Cdd:PRK11658 245 IALVQLAKLEALNARRREIAARYLQALADL 274
 
Name Accession Description Interval E-value
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-358 1.89e-130

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: 377.27  E-value: 1.89e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  17 EIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYLLGA 96
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  97 KVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQSDIG 176
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 177 CFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVENVKDPKTWAMPGFNFRFTDILASIGIEQLKILPERIEYLKEI 256
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 257 YQVYLEGLKDLSINCIPvKIETGEVPVY-------TEYLANDREDFIQNLSKAEIDSRPFYPDLDKASYFPQ----GNRD 325
Cdd:cd00616  241 AERYKELLADLPGIRLP-DVPPGVKHSYhlyvirlDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKllgyPPGD 319

                        330       340       350
                 ....*....|....*....|....*....|...
gi 446150946 326 FPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIK 358
Cdd:cd00616  320 LPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
10-361 3.04e-120

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 351.68  E-value: 3.04e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:COG0399    6 RPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  90 APYLLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFL 169
Cdd:COG0399   86 AILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 170 GTQSDIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVEnvKDPK-TWAMPGFNFRFTDILASIGIEQLKILPE 248
Cdd:COG0399  166 GTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRD--RDAKyEHVELGYNYRMDELQAAIGLAQLKRLDE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 249 RIEYLKEIYQVYLEGLKDLSiNCIPVKIETGEVPVYTEY-----LANDREDFIQNLSKAEIDSRPFYPD-LDKASYF--- 319
Cdd:COG0399  244 FIARRRAIAARYREALADLP-GLTLPKVPPGAEHVYHLYvirldEGEDRDELIAALKARGIGTRVHYPIpLHLQPAYrdl 322

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446150946 320 PQGNRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIKKIY 361
Cdd:COG0399  323 GYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 14-358 3.43e-99

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: 298.04  E-value: 3.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   14 EEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYL 93
Cdd:pfam01041   4 DEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   94 LGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQS 173
Cdd:pfam01041  84 LGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  174 DIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVENVKDPKTWA-MPGFNFRFTDILASIGIEQLKILPERIEY 252
Cdd:pfam01041 164 DAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHeVLGYNYRMTEIQAAIGLAQLERLDEFIAR 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  253 LKEIYQVYLEGLKDLSINCIPVKIETGEV------PVYTEYLANDREDFIQNLSKAEIDSRPFYPDLDK-----ASYFPQ 321
Cdd:pfam01041 244 RREIAALYQTLLADLPGFTPLTTPPEADVhawhlfPILVPEEAINRDELVEALKEAGIGTRVHYPIPLHlqpyyRDLFGY 323

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446150946  322 GNRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIK 358
Cdd:pfam01041 324 APGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 10-360 5.99e-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: 236.46  E-value: 5.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:TIGR03588   5 RQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   90 APYLLGAKVVLVDVESDRPIIDVTKVEEIIT----PRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNN 165
Cdd:TIGR03588  85 CALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  166 RGFLGTQ--SDIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVEnvKDPKTWAMP------------GFNFRF 231
Cdd:TIGR03588 165 GKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGIT--KDPLLFEKQdegpwyyeqqelGFNYRM 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  232 TDILASIGIEQLKILPERIEYLKEIYQVYLEGLKDLSInCIPVKIETGEVPVYTEY-------LANDREDFIQNLSKAEI 304
Cdd:TIGR03588 243 TDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPY-FTPLTIPLGSKSAWHLYpilldqeFGCTRKEVFEALRAAGI 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446150946  305 DSRPFYPDLDKASYFPQG--NRDFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIKKI 360
Cdd:TIGR03588 322 GVQVHYIPVHLQPYYRQGfgDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
10-267 2.55e-55

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 185.61  E-value: 2.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  10 RTSFEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAH 89
Cdd:PRK11658   9 RPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  90 APYLLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSK-NNR-- 166
Cdd:PRK11658  89 MIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYyKGRhi 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 167 GFLGTqsdiGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHGVE-NVKDPKTWA--------MPGFNFRFTDILAS 237
Cdd:PRK11658 169 GARGT----AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGvDAFDRQTQGrapqaevlTPGYKYNLADINAA 244

                        250       260       270
                 ....*....|....*....|....*....|
gi 446150946 238 IGIEQLKILPERIEYLKEIYQVYLEGLKDL 267
Cdd:PRK11658 245 IALVQLAKLEALNARRREIAARYLQALADL 274
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 17-361 7.12e-51

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 173.87  E-value: 7.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  17 EIDRVVNSFKNQNIS-QGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYLLG 95
Cdd:PRK11706  13 ELDYIQQAMSSGKLCgDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  96 AKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQSDI 175
Cdd:PRK11706  93 AKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 176 GCFSLSIAKTITTGQGGFAVTNNSDLAfkLRA--IRTHGVENVK------DPKTWAMPGFNFRFTDILASIGIEQLKILp 247
Cdd:PRK11706 173 GCFSFHETKNYTAGEGGALLINDPALI--ERAeiIREKGTNRSQffrgqvDKYTWVDIGSSYLPSELQAAYLWAQLEAA- 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 248 ERI-EYLKEIYQVYLEGLKDLSINCipvKIETGEVPVYTEYLAN----------DREDFIQNLSKAEIDSrPF-YPDLDK 315
Cdd:PRK11706 250 DRInQRRLALWQRYYDALAPLAEAG---RIELPSIPDDCKHNAHmfyiklrdleDRSALINFLKEAGIMA-VFhYIPLHS 325

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446150946 316 AsyfPQGNR------DFPNSRKYGLKGIYLPSGPSQKIDNIKFVIEQIKKIY 361
Cdd:PRK11706 326 S---PAGERfgrfhgEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFF 374
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 13-268 7.07e-43

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 154.27  E-value: 7.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  13 FEEAEIDRVVNSFKNQNISQGLVTAQFERELSEYLGVKYVIATSSGSTAILLALLAV--------GIRPGDEVIvpnrTW 84
Cdd:PRK15407  42 IDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPGDEVI----TV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  85 IA---TAHAPYL-LGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIPVHLNGRSANMKKLQVICKKNNICLIEDAAQAI 160
Cdd:PRK15407 118 AAgfpTTVNPIIqNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDAL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 161 GSKNNRGFLGTQSDIGCFSLSIAKTITTGQGGFAVTNNSDLAFKLRAIRTHG----VENVKD--------------PK-- 220
Cdd:PRK15407 198 GSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGrdcwCAPGCDntcgkrfgwqlgelPFgy 277

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446150946 221 ----TWAMPGFNFRFTDILASIGIEQLKILPERIEYLKEIYQVYLEGLKDLS 268
Cdd:PRK15407 278 dhkyTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLE 329
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 41-155 1.45e-15

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: 77.09  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  41 RE-LSEYL----GVKY----VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDV-ESDRPII 110
Cdd:COG0436   73 REaIAAYYkrryGVDLdpdeILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLdEENGFLP 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446150946 111 DVTKVEEIITPRTRAIIpvhLN------GRSAN---MKKLQVICKKNNICLIED 155
Cdd:COG0436  152 DPEALEAAITPRTKAIV---LNspnnptGAVYSreeLEALAELAREHDLLVISD 202
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 39-267 7.29e-15

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: 74.69  E-value: 7.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  39 FERELSEYLGVKY--------VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVESDRPI- 109
Cdd:cd00609   41 LREAIAEWLGRRGgvdvppeeIVVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFl 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 110 IDVTKVEEIITPRTRAIIPVHLN---GRSANMKKLQ---VICKKNNICLIEDAA-QAIGSKNNRGFLGTQSDIG-----C 177
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYLNNPNnptGAVLSEEELEelaELAKKHGILIISDEAyAELVYDGEPPPALALLDAYervivL 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 178 FSLSiaKTI-TTG-QGGFAVTNNSDLAFKLRAIrthgvenvKDPKTWAMPGFNFRftdILASIGIEQLKILPERIEYLKE 255
Cdd:cd00609  200 RSFS--KTFgLPGlRIGYLIAPPEELLERLKKL--------LPYTTSGPSTLSQA---AAAAALDDGEEHLEELRERYRR 266

                        250
                 ....*....|..
gi 446150946 256 IYQVYLEGLKDL 267
Cdd:cd00609  267 RRDALLEALKEL 278
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 37-197 6.11e-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: 66.25  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  37 AQFERELSEYL--GVKYVIATSSGSTAILLALLAVGiRPGDEVIVP-----NRTWIATAhapyLLGAKVVLVDV-ESDRP 108
Cdd:cd01494    3 EELEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDanghgSRYWVAAE----LAGAKPVPVPVdDAGYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946 109 IIDVTKVEE-IITPRTRAIIPVHLNGRSA---NMKKLQVICKKNNICLIEDAAQAIGSKNNRGFLGTQSDIGCFSLSIAK 184
Cdd:cd01494   78 GLDVAILEElKAKPNVALIVITPNTTSGGvlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHK 157

                        170
                 ....*....|...
gi 446150946 185 TITTGQGGFAVTN 197
Cdd:cd01494  158 NLGGEGGGVVIVK 170
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
47-155 1.10e-12

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 68.43  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  47 LGVKYVIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLV--DVESDRPIIDVTKVEEIITPRTR 124
Cdd:PRK06108  82 TPPERIAVTSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVplDFGGGGWTLDLDRLLAAITPRTR 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446150946 125 AII---PVHLNGRSANMKKLQVI---CKKNNICLIED 155
Cdd:PRK06108 161 ALFinsPNNPTGWTASRDDLRAIlahCRRHGLWIVAD 197
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 52-155 1.79e-11

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 64.76  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDV-ESDRPIIDVTKVEEIITPRTRAIIpvh 130
Cdd:PRK05764  94 VIVTTGAKQALYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTgEENGFKLTVEQLEAAITPKTKALI--- 169

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446150946 131 LNGRS---------ANMKKLQVICKKNNICLIED 155
Cdd:PRK05764 170 LNSPSnptgavyspEELEAIADVAVEHDIWVLSD 203
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
31-155 5.05e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 57.17  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  31 SQGLVTAqfeRE-LSEY---LGVKY----VIATSSGSTAILLALLAVgIRPGDEVIVPNrtwiaTAHAPY-----LLGAK 97
Cdd:PRK07568  65 SQGIPEL---REaFAKYykkWGIDVepdeILITNGGSEAILFAMMAI-CDPGDEILVPE-----PFYANYngfatSAGVK 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446150946  98 VVLV--DVESDRPIIDVTKVEEIITPRTRAII---PVHLNG---RSANMKKLQVICKKNNICLIED 155
Cdd:PRK07568 136 IVPVttKIEEGFHLPSKEEIEKLITPKTKAILisnPGNPTGvvyTKEELEMLAEIAKKHDLFLISD 201
PRK09082 PRK09082
methionine aminotransferase; Validated
 53-155 2.55e-08

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 54.92  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  53 IATSSGST-AILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAIIpvhL 131
Cdd:PRK09082  94 ITVTAGATeALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLII---L 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446150946 132 NG---------RSANMKKLQVICKKNNICLIED 155
Cdd:PRK09082 170 NTphnpsgtvwSAADMRALWQLIAGTDIYVLSD 202
PRK07550 PRK07550
aminotransferase;
52-155 4.36e-08

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 54.19  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVGiRPGDEVIVPN------RTWIAtahapyLLGAKVVLVDVESDRPII-DVTKVEEIITPRTR 124
Cdd:PRK07550  93 VHITSGCNQAFWAAMVTLA-GAGDEVILPLpwyfnhKMWLD------MLGIRPVYLPCDEGPGLLpDPAAAEALITPRTR 165

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446150946 125 AIIPVHLNGRS------ANMKKLQVICKKNNICLIED 155
Cdd:PRK07550 166 AIALVTPNNPTgvvyppELLHELYDLARRHGIALILD 202
PRK07682 PRK07682
aminotransferase;
41-155 7.28e-08

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 53.59  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  41 RELSEYL----GVKY-----VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVESDRPI-I 110
Cdd:PRK07682  64 QEIAKYLkkrfAVSYdpndeIIVTVGASQALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENEFkV 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446150946 111 DVTKVEEIITPRTRAII---PVHLNGRSANMKKLQ---VICKKNNICLIED 155
Cdd:PRK07682 143 QPAQIEAAITAKTKAILlcsPNNPTGAVLNKSELEeiaVIVEKHDLIVLSD 193
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
37-276 7.59e-08

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 53.46  E-value: 7.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   37 AQFERELSEYLGVKYVIA--------TSSGSTAILLALLAVGIRPGDEVIVPNRTWiaTAHAPY--LLGAKVVLVDVE-S 105
Cdd:pfam00155  42 PELREALAKFLGRSPVLKldreaavvFGSGAGANIEALIFLLANPGDAILVPAPTY--ASYIRIarLAGGEVVRYPLYdS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  106 DRPIIDVTKVEEIITPRTRAII---PVHLNGRSANMKKLQVI---CKKNNICLIEDAAQAIGSKNNRGFLGTQSDIG--- 176
Cdd:pfam00155 120 NDFHLDFDALEAALKEKPKVVLhtsPHNPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVATRALLAegp 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  177 ----CFSLSIAKTITTGQGGFAVTnNSDLAFKLRAIRTHgvenvkdpktwampgfnFRFTDILASIGIEQL-------KI 245
Cdd:pfam00155 200 nllvVGSFSKAFGLAGWRVGYILG-NAAVISQLRKLARP-----------------FYSSTHLQAAAAAALsdpllvaSE 261

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446150946  246 LPERIEYLKEIYQVYLEGLKDLSINCIPVKI 276
Cdd:pfam00155 262 LEEMRQRIKERRDYLRDGLQAAGLSVLPSQA 292
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 36-162 8.03e-08

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: 53.40  E-value: 8.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   36 TAQFE--REL-SEYLGVKY---VIATSSGSTAILLALLAVG--IRPGDEVIVPN-------RTWIATAHapyLLGAKVVL 100
Cdd:pfam00266  42 TQAYEeaREKvAEFINAPSndeIIFTSGTTEAINLVALSLGrsLKPGDEIVITEmehhanlVPWQELAK---RTGARVRV 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446150946  101 VDVESDRpIIDVTKVEEIITPRTRAIIPVHLN---GRSANMKKLQVICKKNNICLIEDAAQAIGS 162
Cdd:pfam00266 119 LPLDEDG-LLDLDELEKLITPKTKLVAITHVSnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
52-157 4.25e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 51.23  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVEsDRPIIDVTKVEEIITPRTRAIIPVHL 131
Cdd:PRK05957  92 IVVTAGSNMAFMNAILAI-TDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIVTISP 169

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446150946 132 NGRS------ANMKKLQVICKKNNICLIEDAA 157
Cdd:PRK05957 170 NNPTgvvypeALLRAVNQICAEHGIYHISDEA 201
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 39-155 4.71e-07

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: 51.05  E-value: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  39 FERELSEYLGVKYVIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIAT----AHAPYLLGAKVVLVDVEsdrpiiDVTK 114
Cdd:cd00614   45 LEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTyrlfERLLPKLGIEVTFVDPD------DPEA 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446150946 115 VEEIITPRTRAII---PVHLNGRSANMKKLQVICKKNNICLIED 155
Cdd:cd00614  118 LEAAIKPETKLVYvesPTNPTLKVVDIEAIAELAHEHGALLVVD 161
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
36-157 2.63e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 48.37  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   36 TAQFERELSEYLGVKYVIATSSGSTAILLALLAVgIRPGDEVIVPNR----TWIATAHApYLLGAKVVLVDVESDrPIID 111
Cdd:pfam01212  34 VNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICGEPahihFDETGGHA-ELGGVQPRPLDGDEA-GNMD 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  112 VTKVEEIITPRTRAIIP----------VHLNG----RSANMKKLQVICKKNNICLIEDAA 157
Cdd:pfam01212 111 LEDLEAAIREVGADIFPptglislentHNSAGgqvvSLENLREIAALAREHGIPVHLDGA 170
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
18-161 4.20e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.21  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  18 IDRVVNSFK--NQNISQGL------VTAQFE--RE-LSEYLGVK---YVIATSSGSTAILLALLAVG-IRPGDEV----- 77
Cdd:COG0520   32 IDAIRDYYEpyNANVHRGAhelsaeATDAYEaaREkVARFIGAAspdEIIFTRGTTEAINLVAYGLGrLKPGDEIlitem 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  78 -----IVPnrtWIATAHApylLGAKVVLVDVESDRpIIDVTKVEEIITPRTRAIIPVHL---NGRSANMKKLQVICKKNN 149
Cdd:COG0520  112 ehhsnIVP---WQELAER---TGAEVRVIPLDEDG-ELDLEALEALLTPRTKLVAVTHVsnvTGTVNPVKEIAALAHAHG 184

                        170
                 ....*....|...
gi 446150946 150 I-CLIeDAAQAIG 161
Cdd:COG0520  185 AlVLV-DGAQSVP 196
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 15-161 5.08e-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: 47.85  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  15 EAEIDRVVNSFK--NQNISQGL------VTAQFE--RE-LSEYLGVKY---VIATSSGSTAILLALLAVG--IRPGDEVI 78
Cdd:cd06453   13 QPVIDAIVDYYRhyNANVHRGVhelsarATDAYEaaREkVARFINAPSpdeIIFTRNTTEAINLVAYGLGraNKPGDEIV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  79 VPN-------RTWIATAHApylLGAKVVLVDVeSDRPIIDVTKVEEIITPRTRAIIPVHLNgrsaN-------MKKLQVI 144
Cdd:cd06453   93 TSVmehhsniVPWQQLAER---TGAKLKVVPV-DDDGQLDLEALEKLLTERTKLVAVTHVS----NvlgtinpVKEIGEI 164

                        170
                 ....*....|....*..
gi 446150946 145 CKKNNICLIEDAAQAIG 161
Cdd:cd06453  165 AHEAGVPVLVDGAQSAG 181
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
39-127 1.52e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 46.64  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  39 FERELSEYLGVKYVIATSSGSTAILLALLAVgIRPGDEVIVpnrtwiataHAPY---------LLGAKVVLVD-VESDRP 108
Cdd:PRK06348  79 YSKNYDLSFKRNEIMATVGACHGMYLALQSI-LDPGDEVII---------HEPYftpykdqieMVGGKPIILEtYEEDGF 148

                         90
                 ....*....|....*....
gi 446150946 109 IIDVTKVEEIITPRTRAII 127
Cdd:PRK06348 149 QINVKKLEALITSKTKAII 167
PRK07683 PRK07683
aminotransferase A; Validated
 52-155 1.84e-05

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 46.26  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVPNRtwIATAHAPY--LLGAKVVLVDVESDRPIIDVTKVEEIITPRTRAII-- 127
Cdd:PRK07683  92 IIVTIGASEAIDIAFRTI-LEPGTEVILPAP--IYPGYEPIirLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlp 168

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446150946 128 -PVHLNGRSANMKKLQVIC---KKNNICLIED 155
Cdd:PRK07683 169 yPSNPTGVTLSKEELQDIAdvlKDKNIFVLSD 200
PRK06107 PRK06107
aspartate transaminase;
35-135 1.98e-05

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 46.27  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  35 VTAQFERELseylGVKY----VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIA-----TAHApyllGAKVVLVDVES 105
Cdd:PRK06107  79 IIAKLERRN----GLHYadneITVGGGAKQAIFLALMAT-LEAGDEVIIPAPYWVSypdmvLAND----GTPVIVACPEE 149

                         90       100       110
                 ....*....|....*....|....*....|
gi 446150946 106 DRPIIDVTKVEEIITPRTRAIIpvhLNGRS 135
Cdd:PRK06107 150 QGFKLTPEALEAAITPRTRWLI---LNAPS 176
PRK08912 PRK08912
aminotransferase;
52-127 3.83e-05

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 45.35  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVpnrtwIATAHAPYL-----LGAKVVLVDVESDRPIIDVTKVEEIITPRTRAI 126
Cdd:PRK08912  90 VMVTSGATEALAAALLAL-VEPGDEVVL-----FQPLYDAYLplirrAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAV 163


                 .
gi 446150946 127 I 127
Cdd:PRK08912 164 L 164
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
43-127 1.16e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 43.64  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  43 LSEYLGVKY----VIATSSGSTAILLALLAVgIRPGDEVIVPnrtwiatahAPYLL-------GAKVVLVDVESDRPI-- 109
Cdd:PRK06836  86 LNRRFGTPLtadhIVMTCGAAGALNVALKAI-LNPGDEVIVF---------APYFVeyrfyvdNHGGKLVVVPTDTDTfq 155

                         90
                 ....*....|....*...
gi 446150946 110 IDVTKVEEIITPRTRAII 127
Cdd:PRK06836 156 PDLDALEAAITPKTKAVI 173
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 41-161 2.34e-04

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 42.73  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  41 RELSEYLGVKY--VIATSSGSTAILLALLAV---GIRPGDEVIVPnrtwiATAH------APYL--LGAKVVLVDVESDr 107
Cdd:COG1104   52 EQVAALLGADPeeIIFTSGGTEANNLAIKGAaraYRKKGKHIITS-----AIEHpavletARFLekEGFEVTYLPVDED- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446150946 108 PIIDVTKVEEIITPRTrAIIPVHLngrsAN--------MKKLQVICKKNNICLIEDAAQAIG 161
Cdd:COG1104  126 GRVDLEALEAALRPDT-ALVSVMH----ANnetgtiqpIAEIAEIAKEHGVLFHTDAVQAVG 182
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 53-155 6.51e-04

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 41.24  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  53 IATSSGSTAILLALLAVgIRPGDEVIVPNRTWIAT----AHAPYLLGAKVVLVDVEsdrpiiDVTKVEEIITPRTRAIIP 128
Cdd:PRK05994  82 LAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSinqfGHAFKSFGWQVRWADAD------DPASFERAITPRTKAIFI 154

                         90       100       110
                 ....*....|....*....|....*....|
gi 446150946 129 VHL---NGRSANMKKLQVICKKNNICLIED 155
Cdd:PRK05994 155 ESIanpGGTVTDIAAIAEVAHRAGLPLIVD 184
Aminotran_3 pfam00202
Aminotransferase class-III;
20-268 6.91e-04

Aminotransferase class-III;


Pssm-ID: 395148 [Multi-domain]  Cd Length: 397  Bit Score: 41.16  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   20 RVVNSFKNQ-----NISQGLVT----AQFERELSEYLGVKYVIATSSGSTAILLAL-LAvgIRPGDEVIVPNRTWIATAH 89
Cdd:pfam00202  47 ALVAAVKTQadklsHVSFGAFTnepaLDLAEKLLKLTPGDRVFLMNSGSEANETAVkLA--RKWYREKGATGRTKIIAFS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946   90 APY-------------------LLGAKVVLV---------DVESDRPIIDVTKVEEIITPRTRAII--PVHLNG-----R 134
Cdd:pfam00202 125 GAFhgrtmgalsvtgskpkyktGFGPFLPGFprlpypdpeFLKEQRCLEELEALIAVKDDEVAAVIvePIQGEGgvnppS 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  135 SANMKKLQVICKKNNICLIEDAAQAIGSKNNRGF----LGTQSDIGCFslsiAKTITTGQGGFAVTNNSDLAfklRAIRT 210
Cdd:pfam00202 205 PGFLAGLRAICKKHGVLLIADEVQTGFGRTGKLFahehWGVPPDIMTF----AKALTGGFPLAATLGRAEVM---QAFAP 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446150946  211 --HGvenvkdpKTWampGFNfrftDILASIGIEQLKIL--PERIEYLKEIYQVYLEGLKDLS 268
Cdd:pfam00202 278 gsHG-------GTF---GGN----PLACAAALATLEIIedEDLLQNAARLGAYLKEGLEDLQ 325
PRK03321 PRK03321
putative aminotransferase; Provisional
 42-127 1.19e-03

putative aminotransferase; Provisional


Pssm-ID: 179559  Cd Length: 352  Bit Score: 40.34  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  42 ELSEYLGVKYV-IATSSGSTAILLALLAVGIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVESDRpIIDVTKVEEIIT 120
Cdd:PRK03321  65 ALAEHLGVPPEhVAVGCGSVALCQQLVQATAGPGDEVIFAWRSFEAYPILVQVAGATPVQVPLTPDH-THDLDAMAAAIT 143


                 ....*..
gi 446150946 121 PRTRAII 127
Cdd:PRK03321 144 DRTRLIF 150
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 39-126 1.42e-03

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 40.40  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  39 FERELSEYLGVKYVIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATahapYLLGAKV-VLVDVESDR-PIIDVTKVE 116
Cdd:PRK07811  66 LEEQLAALEGGAYGRAFSSGMAATDCLLRAV-LRPGDHIVIPNDAYGGT----FRLIDKVfTRWGVEYTPvDLSDLDAVR 140

                         90
                 ....*....|
gi 446150946 117 EIITPRTRAI 126
Cdd:PRK07811 141 AAITPRTKLI 150
tnaA PRK13238
tryptophanase;
39-157 2.68e-03

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 39.41  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  39 FERELSEYLGVKYVIATSSGSTA--ILLALLavgIRPGDevIVPNRTWIAT--AHAPyLLGAKVV-LV-----DVESDRP 108
Cdd:PRK13238  83 LEDAVKDIFGYPYTIPTHQGRAAeqILFPVL---IKKGD--VVPSNYHFDTtrAHIE-LNGATAVdLVidealDTGSRHP 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446150946 109 I---IDVTKVEEIITPRTRAII---------------PVHLngrsANMKKLQVICKKNNICLIEDAA 157
Cdd:PRK13238 157 FkgnFDLEKLEALIEEVGAENVpfivmtitnnsaggqPVSM----ANLRAVYEIAKKYGIPVVIDAA 219
PRK10874 PRK10874
cysteine desulfurase CsdA;
71-124 2.81e-03

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 39.25  E-value: 2.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446150946  71 IRPGDEVIVPNrtwiATAHA---PYLL-----GAKVVLVDVESDRpIIDVTKVEEIITPRTR 124
Cdd:PRK10874 106 LQPGDEIIVSE----AEHHAnlvPWLMvaqqtGAKVVKLPLGADR-LPDVDLLPELITPRTR 162
PRK07337 PRK07337
pyridoxal phosphate-dependent aminotransferase;
52-127 2.82e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180937  Cd Length: 388  Bit Score: 39.27  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVP------NRTWIATAHapyllGAKVVLVDVESDRPIIDVTKVEEIITPRTRA 125
Cdd:PRK07337  93 IVVTAGASAALLLACLAL-VERGDEVLMPdpsypcNRHFVAAAE-----GRPVLVPSGPAERFQLTAADVEAAWGERTRG 166


                 ..
gi 446150946 126 II 127
Cdd:PRK07337 167 VL 168
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 52-131 3.06e-03

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 39.35  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  52 VIATSSGSTAILLALLAVG---IRPGDEVIVPnrtwIATAHA---PYLL-----GAKVVLVDVESDRpIIDVTKVEEIIT 120
Cdd:PLN02855  97 IVFTRNATEAINLVAYTWGlanLKPGDEVILS----VAEHHSnivPWQLvaqktGAVLKFVGLTPDE-VLDVEQLKELLS 171

                         90
                 ....*....|.
gi 446150946 121 PRTRAIIPVHL 131
Cdd:PLN02855 172 EKTKLVATHHV 182
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
52-127 3.83e-03

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 38.87  E-value: 3.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446150946  52 VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDV--ESDRPIIDVTKVEEIITPRTRAII 127
Cdd:PRK07777  88 VLVTVGATEAIAAAVLGL-VEPGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLvpDGRGFALDLDALRAAVTPRTRALI 164
PRK12414 PRK12414
putative aminotransferase; Provisional
 48-155 3.86e-03

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 39.00  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446150946  48 GVKY-----VIATSSGSTAILLALLAVgIRPGDEVIVPNRTWIATAHAPYLLGAKVVLVDVESDRPIIDVTKVEEIITPR 122
Cdd:PRK12414  84 GARYdpaseVTVIASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPR 162

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446150946 123 TRAII------PVHLNGRSANMKKLQVICKKNNICLIED 155
Cdd:PRK12414 163 TRMIIvntphnPSATVFSAADLARLAQLTRNTDIVILSD 201
 
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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