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Conserved domains on  [gi|488473575|ref|WP_002517245|]
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MULTISPECIES: DegT/DnrJ/EryC1/StrS aminotransferase family protein [Cutibacterium]

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];
5-365 0e+00

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 518.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   5 FIPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSF 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYL--GVkHAVAVSSGTAALHLALRALGIGPGDEVITPAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  84 TFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAA 163
Cdd:COG0399   79 TFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 164 SIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEK--RYANEYVGLNNRMTDIHASIGRVQL 241
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 242 TKLAGWTKTRQENAAFLS---SNITEAITPAVPEGYVHVYHQYTIRLEgaTGEERDRFVTALKeEHQVGSGVYYPIPNHR 318
Cdd:COG0399  239 KRLDEFIARRRAIAARYRealADLPGLTLPKVPPGAEHVYHLYVIRLD--EGEDRDELIAALK-ARGIGTRVHYPIPLHL 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 488473575 319 LPSLAPY-APGLELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTC 365
Cdd:COG0399  316 QPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-365 0e+00

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 518.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   5 FIPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSF 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYL--GVkHAVAVSSGTAALHLALRALGIGPGDEVITPAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  84 TFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAA 163
Cdd:COG0399   79 TFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 164 SIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEK--RYANEYVGLNNRMTDIHASIGRVQL 241
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 242 TKLAGWTKTRQENAAFLS---SNITEAITPAVPEGYVHVYHQYTIRLEgaTGEERDRFVTALKeEHQVGSGVYYPIPNHR 318
Cdd:COG0399  239 KRLDEFIARRRAIAARYRealADLPGLTLPKVPPGAEHVYHLYVIRLD--EGEDRDELIAALK-ARGIGTRVHYPIPLHL 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 488473575 319 LPSLAPY-APGLELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTC 365
Cdd:COG0399  316 QPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-363 1.29e-160

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: 453.92  E-value: 1.29e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  17 ERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTFAATGNSVALS 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYL--GVkYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  96 GAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAASIDGKHVGTFGT 175
Cdd:cd00616   79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 176 FGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEKRYAN---EYVGLNNRMTDIHASIGRVQLTKLAGWTKTRQ 252
Cdd:cd00616  159 AGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKyehEILGYNYRLSEIQAAIGLAQLEKLDEIIARRR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 253 ENAAFLS---SNITEAITPAVPEGYVHVYHQYTIRLEGATGEERDRFVTALKEEhQVGSGVYYPIPNHRLPS-LAPYAPG 328
Cdd:cd00616  239 EIAERYKellADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEA-GIETRVHYPPLHHQPPYkKLLGYPP 317

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488473575 329 LELPNTEKVAAECVSLPVHPSLSQADRERIVAAVN 363
Cdd:cd00616  318 GDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 11-362 4.67e-148

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: 422.46  E-value: 4.67e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   11 PILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTFAATG 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYL--GVkHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   90 NSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAASIDGKH 169
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  170 VGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGM----EKRYANEYVGLNNRMTDIHASIGRVQLTKLA 245
Cdd:pfam01041 159 VGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMvrkaDKRYWHEVLGYNYRMTEIQAAIGLAQLERLD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  246 GWTKTRQENAAFLSSNITEA----ITPAVPEGYVHVYHQYTIRLEGaTGEERDRFVTALKeEHQVGSGVYYPIPNHRLP- 320
Cdd:pfam01041 239 EFIARRREIAALYQTLLADLpgftPLTTPPEADVHAWHLFPILVPE-EAINRDELVEALK-EAGIGTRVHYPIPLHLQPy 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 488473575  321 --SLAPYAPGlELPNTEKVAAECVSLPVHPSLSQADRERIVAAV 362
Cdd:pfam01041 317 yrDLFGYAPG-DLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 6-365 2.78e-91

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: 278.83  E-value: 2.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575    6 IPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSqVVDGVHCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTF 85
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAE-YVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   86 AATGNSVALSGAKPVFADVDPVTFTLDPASIEASITD----KTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAH 161
Cdd:TIGR03588  80 VATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  162 AASIDGKHVGT--FGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEKR-------------YANEYVGLN 226
Cdd:TIGR03588 160 GAEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDpllfekqdegpwyYEQQELGFN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  227 NRMTDIHASIGRVQLTKLAGWTKTRQENAAFLSSNITE---AITPAVPEGYVHVYHQYTIRLEGATGEERDRFVTALKeE 303
Cdd:TIGR03588 240 YRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDlpyFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALR-A 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473575  304 HQVGSGVYYpIPNHRLP-SLAPYAPGlELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTC 365
Cdd:TIGR03588 319 AGIGVQVHY-IPVHLQPyYRQGFGDG-DLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
4-366 2.71e-87

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 268.43  E-value: 2.71e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   4 QFIPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSsQVVDGVHCVAVNSGTSALHIGLLASGIGEGDEVIVPSF 83
Cdd:PRK11658   3 DFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFC-QLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  84 TFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAA 163
Cdd:PRK11658  82 TWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 164 SIDGKHVGTFGTfGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGM---------EKRYANEYV---GLNNRMTD 231
Cdd:PRK11658 162 YYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafdrqtQGRAPQAEVltpGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 232 IHASIGRVQLTKLAGWTKTRQENAA-FLSSNITEAITP-AVPE-GYVHVYHQYTIRL-EGATGEERDRFVTALKeEHQVG 307
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAArYLQALADLPFQPlSLPAwPHQHAWHLFIIRVdEERCGISRDALMEALK-ERGIG 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473575 308 SGVYYpipnhRLPSLAPY----APGLELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTCA 366
Cdd:PRK11658 320 TGLHF-----RAAHTQKYyrerFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-365 0e+00

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 518.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   5 FIPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSF 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYL--GVkHAVAVSSGTAALHLALRALGIGPGDEVITPAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  84 TFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAA 163
Cdd:COG0399   79 TFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 164 SIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEK--RYANEYVGLNNRMTDIHASIGRVQL 241
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 242 TKLAGWTKTRQENAAFLS---SNITEAITPAVPEGYVHVYHQYTIRLEgaTGEERDRFVTALKeEHQVGSGVYYPIPNHR 318
Cdd:COG0399  239 KRLDEFIARRRAIAARYRealADLPGLTLPKVPPGAEHVYHLYVIRLD--EGEDRDELIAALK-ARGIGTRVHYPIPLHL 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 488473575 319 LPSLAPY-APGLELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTC 365
Cdd:COG0399  316 QPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-363 1.29e-160

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: 453.92  E-value: 1.29e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  17 ERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTFAATGNSVALS 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYL--GVkYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  96 GAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAASIDGKHVGTFGT 175
Cdd:cd00616   79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 176 FGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEKRYAN---EYVGLNNRMTDIHASIGRVQLTKLAGWTKTRQ 252
Cdd:cd00616  159 AGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKyehEILGYNYRLSEIQAAIGLAQLEKLDEIIARRR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 253 ENAAFLS---SNITEAITPAVPEGYVHVYHQYTIRLEGATGEERDRFVTALKEEhQVGSGVYYPIPNHRLPS-LAPYAPG 328
Cdd:cd00616  239 EIAERYKellADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEA-GIETRVHYPPLHHQPPYkKLLGYPP 317

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488473575 329 LELPNTEKVAAECVSLPVHPSLSQADRERIVAAVN 363
Cdd:cd00616  318 GDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 11-362 4.67e-148

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: 422.46  E-value: 4.67e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   11 PILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTFAATG 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYL--GVkHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   90 NSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAASIDGKH 169
Cdd:pfam01041  79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  170 VGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGM----EKRYANEYVGLNNRMTDIHASIGRVQLTKLA 245
Cdd:pfam01041 159 VGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMvrkaDKRYWHEVLGYNYRMTEIQAAIGLAQLERLD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  246 GWTKTRQENAAFLSSNITEA----ITPAVPEGYVHVYHQYTIRLEGaTGEERDRFVTALKeEHQVGSGVYYPIPNHRLP- 320
Cdd:pfam01041 239 EFIARRREIAALYQTLLADLpgftPLTTPPEADVHAWHLFPILVPE-EAINRDELVEALK-EAGIGTRVHYPIPLHLQPy 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 488473575  321 --SLAPYAPGlELPNTEKVAAECVSLPVHPSLSQADRERIVAAV 362
Cdd:pfam01041 317 yrDLFGYAPG-DLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 6-365 2.78e-91

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: 278.83  E-value: 2.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575    6 IPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSSqVVDGVHCVAVNSGTSALHIGLLASGIGEGDEVIVPSFTF 85
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAE-YVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   86 AATGNSVALSGAKPVFADVDPVTFTLDPASIEASITD----KTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAH 161
Cdd:TIGR03588  80 VATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  162 AASIDGKHVGT--FGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEKR-------------YANEYVGLN 226
Cdd:TIGR03588 160 GAEYGGKPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDpllfekqdegpwyYEQQELGFN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  227 NRMTDIHASIGRVQLTKLAGWTKTRQENAAFLSSNITE---AITPAVPEGYVHVYHQYTIRLEGATGEERDRFVTALKeE 303
Cdd:TIGR03588 240 YRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDlpyFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEALR-A 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473575  304 HQVGSGVYYpIPNHRLP-SLAPYAPGlELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTC 365
Cdd:TIGR03588 319 AGIGVQVHY-IPVHLQPyYRQGFGDG-DLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
4-366 2.71e-87

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 268.43  E-value: 2.71e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   4 QFIPPAKPILGDDERKAVDEVIASGMVAQGPQVHAFEDEFSsQVVDGVHCVAVNSGTSALHIGLLASGIGEGDEVIVPSF 83
Cdd:PRK11658   3 DFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFC-QLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  84 TFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAA 163
Cdd:PRK11658  82 TWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 164 SIDGKHVGTFGTfGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGM---------EKRYANEYV---GLNNRMTD 231
Cdd:PRK11658 162 YYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafdrqtQGRAPQAEVltpGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 232 IHASIGRVQLTKLAGWTKTRQENAA-FLSSNITEAITP-AVPE-GYVHVYHQYTIRL-EGATGEERDRFVTALKeEHQVG 307
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAArYLQALADLPFQPlSLPAwPHQHAWHLFIIRVdEERCGISRDALMEALK-ERGIG 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473575 308 SGVYYpipnhRLPSLAPY----APGLELPNTEKVAAECVSLPVHPSLSQADRERIVAAVNTCA 366
Cdd:PRK11658 320 TGLHF-----RAAHTQKYyrerFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 6-362 9.11e-77

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 241.28  E-value: 9.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   6 IPPAKPILGDDERKAVDEVIASGMVA-QGP---QVHA-FEDEFSSQvvdgvHCVAVNSGTSALHIGLLASGIGEGDEVIV 80
Cdd:PRK11706   2 IPFNKPPVVGTELDYIQQAMSSGKLCgDGGftrRCQQwLEQRFGSA-----KVLLTPSCTAALEMAALLLDIQPGDEVIM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  81 PSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHGLKIFEDCAQA 160
Cdd:PRK11706  77 PSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 161 HAASIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGMEKR-----YANEY----VGLNNRMTD 231
Cdd:PRK11706 157 VMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSqffrgQVDKYtwvdIGSSYLPSE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 232 IHAS--------IGRVQLTKLAGWTKTRQENAAFLSSNITEaiTPAVPEGYVHVYHQYTIRLegATGEERDRFVTALKeE 303
Cdd:PRK11706 237 LQAAylwaqleaADRINQRRLALWQRYYDALAPLAEAGRIE--LPSIPDDCKHNAHMFYIKL--RDLEDRSALINFLK-E 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473575 304 HQVGSGVYYpIPNHRLPSLAPY--APGlELPNTEKVAAECVSLPVHPSLSQADRERIVAAV 362
Cdd:PRK11706 312 AGIMAVFHY-IPLHSSPAGERFgrFHG-EDRYTTKESERLLRLPLFYNLTDVEQRTVIDTI 370
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 6-367 3.40e-55

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 187.01  E-value: 3.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   6 IPPAKPILGDDERKA-VDeviAS--GMVAQGPQVHAFEDEFSSQVvdGV-HCVAVNSGTSAlhiGLLA-----------S 70
Cdd:PRK15407  35 IPPSGKVIDAKELQNlVD---ASldFWLTTGRFNDAFEKKLAEFL--GVrYALLVNSGSSA---NLLAfsaltspklgdR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  71 GIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIMPVHLYGLPANMAEIVAIATKHG 150
Cdd:PRK15407 107 ALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHN 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 151 LKIFEDCAQAHAASIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITTSDPEIARKAAMLRNQGME------------KR- 217
Cdd:PRK15407 187 LWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRDcwcapgcdntcgKRf 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 218 ----------YANEYV----GLNNRMTDIHASIGRVQLTKLAGWTKTRQENAAFLSS---------NITEAITPAVPE-- 272
Cdd:PRK15407 267 gwqlgelpfgYDHKYTyshlGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEglasledflILPEATPNSDPSwf 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 273 GYVhvyhqYTIRlEGAtGEERDRFVTALkEEHQVGSGV----------YYPIPNHRLPSlapyapglELPNTEKVAAECV 342
Cdd:PRK15407 347 GFP-----ITVK-EDA-GFTRVELVKYL-EENKIGTRLlfagnltrqpYFKGVKYRVVG--------ELTNTDRIMNDTF 410

                        410       420
                 ....*....|....*....|....*
gi 488473575 343 SLPVHPSLSQADRERIVAAVNTCAK 367
Cdd:PRK15407 411 WIGVYPGLTEEMLDYVIEKIEEFFG 435
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 54-188 7.12e-12

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: 65.92  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSGTSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVT-FTLDPASIEASITDKTAAImpvhL 132
Cdd:COG0436   94 LVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEALEAAITPRTKAI----V 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473575 133 YGLPAN----------MAEIVAIATKHGLKI----------FEDCAQAHAASIDGKHVGTFgTFGAFSfyptK--NMT 188
Cdd:COG0436  169 LNSPNNptgavysreeLEALAELAREHDLLVisdeiyeelvYDGAEHVSILSLPGLKDRTI-VINSFS----KsyAMT 241
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 54-156 1.35e-11

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 65.15  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSGTS-ALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVT-FTLDPASIEASITDKTAAIM--- 128
Cdd:PRK05764  94 VIVTTGAKqALYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIlns 172

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488473575 129 ---PV-HLYGlPANMAEIVAIATKHGLKIFED 156
Cdd:PRK05764 173 psnPTgAVYS-PEELEAIADVAVEHDIWVLSD 203
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 54-197 1.92e-10

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: 58.93  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSGTSALHIGLLASGiGEGDEVIVPS-FTFAATGNSVALSGAKPVFADVDPVTFTLDPASI--EASITDKTAAIM-- 128
Cdd:cd01494   21 VFVPSGTGANEAALLALL-GPGDEVIVDAnGHGSRYWVAAELAGAKPVPVPVDDAGYGGLDVAIleELKAKPNVALIVit 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 129 -PVHLYGLPANMAEIVAIATKHGLKIFEDCAQAHAASIDGKHVGTFGTFGAFSFYPTKNMTSGEGGMITT 197
Cdd:cd01494  100 pNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVVIV 169
PRK07682 PRK07682
aminotransferase;
56-156 2.78e-10

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 61.29  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  56 VNSGTS-ALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVT-FTLDPASIEASITDKTAAIM----- 128
Cdd:PRK07682  86 VTVGASqALDVAMRAI-INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcspn 164

                         90       100
                 ....*....|....*....|....*....
gi 488473575 129 -PVHLYGLPANMAEIVAIATKHGLKIFED 156
Cdd:PRK07682 165 nPTGAVLNKSELEEIAVIVEKHDLIVLSD 193
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 54-209 4.45e-09

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: 57.35  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSGTSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPV-TFTLDPASIEASITDKTAAIMPVHl 132
Cdd:cd00609   63 VVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLYLNN- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575 133 yglPAN----------MAEIVAIATKHGLKIFEDCA---------QAHAASIDGKHVGTFgTFGAFSfyptK--NMTSGE 191
Cdd:cd00609  141 ---PNNptgavlseeeLEELAELAKKHGILIISDEAyaelvydgePPPALALLDAYERVI-VLRSFS----KtfGLPGLR 212

                        170
                 ....*....|....*...
gi 488473575 192 GGMITTSDPEIARKAAML 209
Cdd:cd00609  213 IGYLIAPPEELLERLKKL 230
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
60-182 2.77e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 55.11  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  60 TSALHIGLLA--SGIGEGDEVIVPSFTFAATGNSVALSGAKPVFAD-VDPVTFTLDPASIEASITDKTAAIM------PV 130
Cdd:PRK06348  96 VGACHGMYLAlqSILDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnspnnPT 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488473575 131 HLYGLPANMAEIVAIATKHGLKIFEDcaqahaasidgkhvgtfGTFGAFSFY 182
Cdd:PRK06348 176 GAVFSKETLEEIAKIAIEYDLFIISD-----------------EVYDGFSFY 210
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
75-127 3.65e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 51.73  E-value: 3.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488473575  75 GDEVIVPSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAI 127
Cdd:PRK06836 120 GDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAV 172
PRK08363 PRK08363
alanine aminotransferase; Validated
 54-172 7.36e-07

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 50.58  E-value: 7.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSG-TSALHIgLLASGIGEGDEVIVPSFTFAATGNSVALSGAKPV-FADVDPVTFTLDPASIEASITDKTAAIMPVH 131
Cdd:PRK08363  96 VRVTAAvTEALQL-IFGALLDPGDEILIPGPSYPPYTGLVKFYGGVPVeYRTIEEEGWQPDIDDIRKKITEKTKAIAVIN 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488473575 132 lyglPAN----------MAEIVAIATKHGLKIFEDcAQAHAASIDGKHVGT 172
Cdd:PRK08363 175 ----PNNptgalyekktLKEILDIAGEHDLPVISD-EIYDLMTYEGKHVSP 220
PRK09265 PRK09265
aminotransferase AlaT; Validated
 75-156 1.89e-06

aminotransferase AlaT; Validated


Pssm-ID: 181738  Cd Length: 404  Bit Score: 49.42  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  75 GDEVIVPSFTFAATGNSVALSGAKPVF------ADVDPvtftlDPASIEASITDKTAAIMPVHlyglPAN---------- 138
Cdd:PRK09265 119 GDEVLVPAPDYPLWTAAVSLSGGKPVHylcdeeAGWFP-----DLDDIRSKITPRTKAIVIIN----PNNptgavyskel 189

                         90
                 ....*....|....*...
gi 488473575 139 MAEIVAIATKHGLKIFED 156
Cdd:PRK09265 190 LEEIVEIARQHNLIIFAD 207
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
54-213 7.46e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 47.30  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   54 VAVNSGTSALHIGLLASGIGEGDEVIVPSFTFAATGNSVALSGAKPV-FADVDPVTFTLDPASIEASITDKTAAImpvhL 132
Cdd:pfam00155  66 VVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVrYPLYDSNDFHLDFDALEAALKEKPKVV----L 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  133 YGLPANM----------AEIVAIATKHGLKIFEDCAQAH-------AASI-----DGKHVGTFGTFG-AFSFYptknmts 189
Cdd:pfam00155 142 HTSPHNPtgtvatleelEKLLDLAKEHNILLLVDEAYAGfvfgspdAVATrallaEGPNLLVVGSFSkAFGLA------- 214

                         170       180
                  ....*....|....*....|....
gi 488473575  190 GEGGMITTSDPEIARKAAMLRNQG 213
Cdd:pfam00155 215 GWRVGYILGNAAVISQLRKLARPF 238
PRK09082 PRK09082
methionine aminotransferase; Validated
 48-128 1.68e-05

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 46.45  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  48 VDGVHCVAVNSG-TSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAA 126
Cdd:PRK09082  88 YDADSEITVTAGaTEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRL 166


                 ..
gi 488473575 127 IM 128
Cdd:PRK09082 167 II 168
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
65-160 2.38e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 45.90  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  65 IGLLASGIG---EGDEVIV-----PSfTFAATGNSVALSGAKPVFADVDPvTFTLDPASIEASITDKTAAIMPVHL---Y 133
Cdd:COG0520   90 INLVAYGLGrlkPGDEILItemehHS-NIVPWQELAERTGAEVRVIPLDE-DGELDLEALEALLTPRTKLVAVTHVsnvT 167

                         90       100
                 ....*....|....*....|....*..
gi 488473575 134 GLPANMAEIVAIATKHGLKIFEDCAQA 160
Cdd:COG0520  168 GTVNPVKEIAALAHAHGALVLVDGAQS 194
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
52-156 2.85e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 45.70  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  52 HCVAVNSGTSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVT--FTLDPASIEASITDKTAAIMp 129
Cdd:PRK06108  86 RIAVTSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGGggWTLDLDRLLAAITPRTRALF- 163

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488473575 130 vhlYGLPAN----------MAEIVAIATKHGLKIFED 156
Cdd:PRK06108 164 ---INSPNNptgwtasrddLRAILAHCRRHGLWIVAD 197
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 65-160 4.11e-05

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: 45.15  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  65 IGLLASGIG----EGDEVIVPSFTFAAtgNSVAL------SGAKPVFADVDPvTFTLDPASIEASITDKTAAIMPVHL-- 132
Cdd:cd06453   74 INLVAYGLGrankPGDEIVTSVMEHHS--NIVPWqqlaerTGAKLKVVPVDD-DGQLDLEALEKLLTERTKLVAVTHVsn 150

                         90       100
                 ....*....|....*....|....*....
gi 488473575 133 -YGLPANMAEIVAIATKHGLKIFEDCAQA 160
Cdd:cd06453  151 vLGTINPVKEIGEIAHEAGVPVLVDGAQS 179
PRK07683 PRK07683
aminotransferase A; Validated
 74-127 5.26e-05

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 44.71  E-value: 5.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488473575  74 EGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAI 127
Cdd:PRK07683 112 PGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCV 165
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
56-214 8.25e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 43.74  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575   56 VNSGTSALHIGLLASgIGEGDEVIV--PSFTFA-ATGNSVALSGAKPVFADVDPvTFTLDPASIEASITDKTAAIMP--- 129
Cdd:pfam01212  53 VPSGTAANQLALMAH-CQRGDEVICgePAHIHFdETGGHAELGGVQPRPLDGDE-AGNMDLEDLEAAIREVGADIFPptg 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  130 -------VHLYG----LPANMAEIVAIATKHGLKIFEDCAQ-AHAASIDGKHVGT-FGTFGAFSFYPTKNMTSGEGGMIT 196
Cdd:pfam01212 131 lislentHNSAGgqvvSLENLREIAALAREHGIPVHLDGARfANAAVALGVIVKEiTSYADSVTMCLSKGLGAPVGSVLA 210

                         170       180
                  ....*....|....*....|....*
gi 488473575  197 TSDPEIARK-------AAMLRNQGM 214
Cdd:pfam01212 211 GSDDFIAKAirqrkylGGGLRQAGV 235
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
57-156 8.33e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 44.07  E-value: 8.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  57 NSGTSALHIGLLASgIGEGDEVIVPSfTFAATGNSVA-LSGAK--PVFADVDPvTFTLDP-ASIEASITDKTAAIMPVHl 132
Cdd:PRK07568  95 NGGSEAILFAMMAI-CDPGDEILVPE-PFYANYNGFAtSAGVKivPVTTKIEE-GFHLPSkEEIEKLITPKTKAILISN- 170

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488473575 133 yglPAN----------MAEIVAIATKHGLKIFED 156
Cdd:PRK07568 171 ---PGNptgvvytkeeLEMLAEIAKKHDLFLISD 201
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 75-156 2.44e-04

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 42.80  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  75 GDEVIVPSFTFAATGNSVALSGAKPVFADVD------PvtftlDPASIEASITDKTAAIMPVHlyglPAN---------- 138
Cdd:PRK13355 232 GDEVLIPSPDYPLWTACVNLAGGTAVHYRCDeqsewyP-----DIDDIRSKITSRTKAIVIIN----PNNptgalyprev 302

                         90
                 ....*....|....*...
gi 488473575 139 MAEIVAIATKHGLKIFED 156
Cdd:PRK13355 303 LQQIVDIAREHQLIIFSD 320
PRK07550 PRK07550
aminotransferase;
54-151 4.78e-04

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 41.87  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  54 VAVNSGTSALHIGLLASGIGEGDEVIVPS-FTFaatgN---SVALSGAKPVFADVDPV-TFTLDPASIEASITDKTAAIM 128
Cdd:PRK07550  93 VHITSGCNQAFWAAMVTLAGAGDEVILPLpWYF----NhkmWLDMLGIRPVYLPCDEGpGLLPDPAAAEALITPRTRAIA 168

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488473575 129 PVHlyglPAN----------MAEIVAIATKHGL 151
Cdd:PRK07550 169 LVT----PNNptgvvyppelLHELYDLARRHGI 197
PRK08912 PRK08912
aminotransferase;
54-128 1.78e-03

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 39.96  E-value: 1.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473575  54 VAVNSG-TSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVTFTLDPASIEASITDKTAAIM 128
Cdd:PRK08912  90 VMVTSGaTEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVL 164
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 49-156 3.26e-03

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 39.31  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  49 DGVHCVAVNSGTSALHIgLLASGIGEGDEVIVPSFTFAATGNSVALS----GAKPVFADVDpvtftlDPASIEASITDKT 124
Cdd:PRK05994  77 GGTAALAVASGHAAQFL-VFHTLLQPGDEFIAARKLYGGSINQFGHAfksfGWQVRWADAD------DPASFERAITPRT 149

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488473575 125 AAIMPVHLY---GLPANMAEIVAIATKHGLKIFED 156
Cdd:PRK05994 150 KAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
53-127 3.52e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 39.28  E-value: 3.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473575  53 CVAVNSGTS-ALHIGLLAsgIGE-GDEVIVPSFTFAATGNSVALSGAKPVFADVDPvTFTLDPASIEASITDKTAAI 127
Cdd:PRK05957  91 AIVVTAGSNmAFMNAILA--ITDpGDEIILNTPYYFNHEMAITMAGCQPILVPTDD-NYQLQPEAIEQAITPKTRAI 164
PRK06107 PRK06107
aspartate transaminase;
39-124 7.00e-03

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 38.18  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473575  39 FEDEFSSQVVDGVHCVAvNSGTSALHIGLLASgIGEGDEVIVPSFTFAATGNSVALSGAKPVFADVDPVT-FTLDPASIE 117
Cdd:PRK06107  83 LERRNGLHYADNEITVG-GGAKQAIFLALMAT-LEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLTPEALE 160


                 ....*..
gi 488473575 118 ASITDKT 124
Cdd:PRK06107 161 AAITPRT 167
argD PRK03715
acetylornithine transaminase protein; Provisional
 112-160 8.70e-03

acetylornithine transaminase protein; Provisional


Pssm-ID: 179636 [Multi-domain]  Cd Length: 395  Bit Score: 37.74  E-value: 8.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488473575 112 DPASIEASITDKTAAIM--PVHLYG--LPAN---MAEIVAIATKHGLKIFEDCAQA 160
Cdd:PRK03715 168 DIASVEKLITDKTVAVMlePVQGEGgvIPATrefMQQLRALTKQHGLLLIVDEVQT 223
 
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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