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Conserved domains on  [gi|169811288|gb|ACA85872|]
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DegT/DnrJ/EryC1/StrS aminotransferase [Shewanella woodyi ATCC 51908]

Protein Classification

LegC family aminotransferase( domain architecture ID 10024510)

LegC family aminotransferase belongs to the larger DegT/DnrJ/EryC1/StrS family of aminotransferases that catalyze pyridoxal-phosphate-dependent amino transfer

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
18-376 0e+00

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


:

Pssm-ID: 275034  Cd Length: 359  Bit Score: 611.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   18 IPLHAPTFAGNEQAYVAETITSTFVSSVGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTF 97
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   98 VATCNALYHMGAAPIFVDISTVSLGLSPQAVQTYLEEYGLLNEeGLCIHKETKQTIKAVMPMHTFGHPVELDELVLICQQ 177
Cdd:TIGR04181  81 VATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERKD-GVLINKETGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  178 WNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPYEFYHDEAGF 257
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPWEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  258 NYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDG-GELLFVQEPSYAKSNYWLNAVICPNLHSRDKLLKLTNDSG 336
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGiPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 169811288  337 VMTRPVWQLMHRLPMFKDALRGSLQHSEWFEERLVNLPSS 376
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
 
Name Accession Description Interval E-value
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
18-376 0e+00

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


Pssm-ID: 275034  Cd Length: 359  Bit Score: 611.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   18 IPLHAPTFAGNEQAYVAETITSTFVSSVGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTF 97
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   98 VATCNALYHMGAAPIFVDISTVSLGLSPQAVQTYLEEYGLLNEeGLCIHKETKQTIKAVMPMHTFGHPVELDELVLICQQ 177
Cdd:TIGR04181  81 VATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERKD-GVLINKETGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  178 WNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPYEFYHDEAGF 257
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPWEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  258 NYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDG-GELLFVQEPSYAKSNYWLNAVICPNLHSRDKLLKLTNDSG 336
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGiPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 169811288  337 VMTRPVWQLMHRLPMFKDALRGSLQHSEWFEERLVNLPSS 376
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
17-377 3.31e-116

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 342.05  E-value: 3.31e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  17 FIPLHAPTFAGNEQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLT 96
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  97 FVATCNALYHMGAAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQ 176
Cdd:COG0399   80 FVATANAILYVGATPVFVDIDPDTYNIDPEAL-----------EAAI-----TPRT-KAIIPVHLYGQPADMDAIMAIAK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 177 QWNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPyEFYHDEAG 256
Cdd:COG0399  143 KHGLKVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-KYEHVELG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 257 FNYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDG-GELLFVQEPSYAKSNYWLNAVICPNLHSRDKLLKLTNDS 335
Cdd:COG0399  222 YNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADlPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKAR 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 169811288 336 GVMTRPVWQL-MHRLPMFKDAL--RGSLQHSEWFEERLVNLPSSP 377
Cdd:COG0399  302 GIGTRVHYPIpLHLQPAYRDLGyrPGDLPVAERLAERVLSLPLHP 346
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
29-380 1.40e-99

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: 299.46  E-value: 1.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  29 EQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCNALYHMG 108
Cdd:cd00616    1 ELEAVEEVLDSGWLTL-GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 109 AAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQQWNLVLIEDAAE 188
Cdd:cd00616   80 ATPVFVDIDPDTYNIDPELI-----------EAAI-----TPRT-KAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 189 SLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPYEFYHDEAGFNYRMPNLNAAL 268
Cdd:cd00616  143 ALGATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAI 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 269 GCAQMESLPLFIEQKRALAMHYNSFF-DGGELLFVQEPSYAKSNYWLNAVICPNL--HSRDKLLKLTNDSGVMTRPVWQL 345
Cdd:cd00616  223 GLAQLEKLDEIIARRREIAERYKELLaDLPGIRLPDVPPGVKHSYHLYVIRLDPEagESRDELIEALKEAGIETRVHYPP 302
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 169811288 346 MHRLPMFKDAL---RGSLQHSEWFEERLVNLPSSPINT 380
Cdd:cd00616  303 LHHQPPYKKLLgypPGDLPNAEDLAERVLSLPLHPSLT 340
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
23-377 4.81e-86

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: 264.92  E-value: 4.81e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   23 PTFAGNEQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCN 102
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  103 ALYHMGAAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQQWNLVL 182
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAI-----------EAAI-----TPRT-KAIIPVHLYGQPADMDAIRAIAARHGLPV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  183 IEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNnqaNGIRAKHITTT----AKVPHPYEFYHDEAGFN 258
Cdd:pfam01041 143 IEDAAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTN---DPELAEKARVLrnhgMVRKADKRYWHEVLGYN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  259 YRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDGGELLFVQE--PSYAKSNYWLNAVICPN-LHSRDKLLKLTNDS 335
Cdd:pfam01041 220 YRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTtpPEADVHAWHLFPILVPEeAINRDELVEALKEA 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 169811288  336 GVMTRPV-WQLMHRLPMFKDA---LRGSLQHSEWFEERLVNLPSSP 377
Cdd:pfam01041 300 GIGTRVHyPIPLHLQPYYRDLfgyAPGDLPNAEDISSRVLSLPLYP 345
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
18-374 2.04e-46

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 162.70  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  18 IPLHAPTFAGNEQAYVAETITSTFVSSVGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTF 97
Cdd:PRK11706   2 IPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  98 VATCNALYHMGAAPIFVDISTVSLGLSPQAVQtyleeygllneeglciHKETKQTiKAVMPMHTFGHPVELDELVLICQQ 177
Cdd:PRK11706  82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIE----------------AAITPKT-RAIVPVHYAGVACEMDTIMALAKK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 178 WNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHI----TTTAKvphpyeFYHD 253
Cdd:PRK11706 145 HNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIrekgTNRSQ------FFRG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 254 EA--------GFNYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFF----DGGELLFVQEPSYAKSNYWLNAVICPN 321
Cdd:PRK11706 219 QVdkytwvdiGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALaplaEAGRIELPSIPDDCKHNAHMFYIKLRD 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169811288 322 LHSRDKLLKLTNDSGVMTR----PvwqlMHRLPMFKDALR--GSLQHSEWFEERLVNLP 374
Cdd:PRK11706 299 LEDRSALINFLKEAGIMAVfhyiP----LHSSPAGERFGRfhGEDRYTTKESERLLRLP 353
 
Name Accession Description Interval E-value
NHT_00031 TIGR04181
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ...
18-376 0e+00

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


Pssm-ID: 275034  Cd Length: 359  Bit Score: 611.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   18 IPLHAPTFAGNEQAYVAETITSTFVSSVGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTF 97
Cdd:TIGR04181   1 IPLHEPNFGGNEKKYVKECIDSGWVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   98 VATCNALYHMGAAPIFVDISTVSLGLSPQAVQTYLEEYGLLNEeGLCIHKETKQTIKAVMPMHTFGHPVELDELVLICQQ 177
Cdd:TIGR04181  81 VATANAISYLGAEPVFVDVDPDTLGLDPDALEEFLEEEAERKD-GVLINKETGRRIKACVPVHVFGHPADMDEIMEICDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  178 WNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPYEFYHDEAGF 257
Cdd:TIGR04181 160 WNLPVVEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPHPWEFEHDEVGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  258 NYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDG-GELLFVQEPSYAKSNYWLNAVICPNLHSRDKLLKLTNDSG 336
Cdd:TIGR04181 240 NYRMPNINAALGCAQLEQLEEFLARKRELAEIYKEFFSGiPGVEFLPEPAGARSNYWLNALLLDSKLDRDELLEALNENG 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 169811288  337 VMTRPVWQLMHRLPMFKDALRGSLQHSEWFEERLVNLPSS 376
Cdd:TIGR04181 320 IQTRPLWTLMHELPMYRDCPRDDLPVAENLEERLINLPSS 359
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
17-377 3.31e-116

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 342.05  E-value: 3.31e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  17 FIPLHAPTFAGNEQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLT 96
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  97 FVATCNALYHMGAAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQ 176
Cdd:COG0399   80 FVATANAILYVGATPVFVDIDPDTYNIDPEAL-----------EAAI-----TPRT-KAIIPVHLYGQPADMDAIMAIAK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 177 QWNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPyEFYHDEAG 256
Cdd:COG0399  143 KHGLKVIEDAAQALGATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-KYEHVELG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 257 FNYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDG-GELLFVQEPSYAKSNYWLNAVICPNLHSRDKLLKLTNDS 335
Cdd:COG0399  222 YNYRMDELQAAIGLAQLKRLDEFIARRRAIAARYREALADlPGLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKAR 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 169811288 336 GVMTRPVWQL-MHRLPMFKDAL--RGSLQHSEWFEERLVNLPSSP 377
Cdd:COG0399  302 GIGTRVHYPIpLHLQPAYRDLGyrPGDLPVAERLAERVLSLPLHP 346
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
29-380 1.40e-99

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: 299.46  E-value: 1.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  29 EQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCNALYHMG 108
Cdd:cd00616    1 ELEAVEEVLDSGWLTL-GPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 109 AAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQQWNLVLIEDAAE 188
Cdd:cd00616   80 ATPVFVDIDPDTYNIDPELI-----------EAAI-----TPRT-KAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 189 SLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHITTTAKVPHPYEFYHDEAGFNYRMPNLNAAL 268
Cdd:cd00616  143 ALGATYKGRKVGTFGDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDRFKYEHEILGYNYRLSEIQAAI 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 269 GCAQMESLPLFIEQKRALAMHYNSFF-DGGELLFVQEPSYAKSNYWLNAVICPNL--HSRDKLLKLTNDSGVMTRPVWQL 345
Cdd:cd00616  223 GLAQLEKLDEIIARRREIAERYKELLaDLPGIRLPDVPPGVKHSYHLYVIRLDPEagESRDELIEALKEAGIETRVHYPP 302
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 169811288 346 MHRLPMFKDAL---RGSLQHSEWFEERLVNLPSSPINT 380
Cdd:cd00616  303 LHHQPPYKKLLgypPGDLPNAEDLAERVLSLPLHPSLT 340
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
23-377 4.81e-86

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: 264.92  E-value: 4.81e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   23 PTFAGNEQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCN 102
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  103 ALYHMGAAPIFVDISTVSLGLSPQAVqtyleeygllnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQQWNLVL 182
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAI-----------EAAI-----TPRT-KAIIPVHLYGQPADMDAIRAIAARHGLPV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  183 IEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNnqaNGIRAKHITTT----AKVPHPYEFYHDEAGFN 258
Cdd:pfam01041 143 IEDAAHALGATYQGKKVGTLGDAATFSFHPTKNLTTGEGGAVVTN---DPELAEKARVLrnhgMVRKADKRYWHEVLGYN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  259 YRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDGGELLFVQE--PSYAKSNYWLNAVICPN-LHSRDKLLKLTNDS 335
Cdd:pfam01041 220 YRMTEIQAAIGLAQLERLDEFIARRREIAALYQTLLADLPGFTPLTtpPEADVHAWHLFPILVPEeAINRDELVEALKEA 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 169811288  336 GVMTRPV-WQLMHRLPMFKDA---LRGSLQHSEWFEERLVNLPSSP 377
Cdd:pfam01041 300 GIGTRVHyPIPLHLQPYYRDLfgyAPGDLPNAEDISSRVLSLPLYP 345
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
33-377 9.53e-62

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: 202.94  E-value: 9.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288   33 VAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCNALYHMGAAPI 112
Cdd:TIGR03588  16 VVEVLKSDFLTQ-GPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  113 FVDISTVSLGLSPQAVqtyleeygllnEEGLCIHKETKqtIKAVMPMHTFGHPVELDELVLICQQWNLVLIEDAAESLGS 192
Cdd:TIGR03588  95 FVDIDPDTGNIDEDAL-----------EKKLAAAKGKL--PKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  193 RYKEKHTGTI--GEFAALSFNGNKIITTGGGGVLLTNNQA----------NGIRAKHITTTAKVPHPYEFYHDEAGFNYR 260
Cdd:TIGR03588 162 EYGGKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEElaermrllrsHGITKDPLLFEKQDEGPWYYEQQELGFNYR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  261 MPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDGGEL-LFVQEPSYAKSNYWLnAVICPNLH---SRDKLLKLTNDSG 336
Cdd:TIGR03588 242 MTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYfTPLTIPLGSKSAWHL-YPILLDQEfgcTRKEVFEALRAAG 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 169811288  337 VMTRPVWQLMHRLPMFKDAL-RGSLQHSEWFEERLVNLPSSP 377
Cdd:TIGR03588 321 IGVQVHYIPVHLQPYYRQGFgDGDLPSAENFYLAEISLPLHP 362
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
18-374 2.04e-46

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 162.70  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  18 IPLHAPTFAGNEQAYVAETITSTFVSSVGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTF 97
Cdd:PRK11706   2 IPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  98 VATCNALYHMGAAPIFVDISTVSLGLSPQAVQtyleeygllneeglciHKETKQTiKAVMPMHTFGHPVELDELVLICQQ 177
Cdd:PRK11706  82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIE----------------AAITPKT-RAIVPVHYAGVACEMDTIMALAKK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 178 WNLVLIEDAAESLGSRYKEKHTGTIGEFAALSFNGNKIITTGGGGVLLTNNQANGIRAKHI----TTTAKvphpyeFYHD 253
Cdd:PRK11706 145 HNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIrekgTNRSQ------FFRG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 254 EA--------GFNYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFF----DGGELLFVQEPSYAKSNYWLNAVICPN 321
Cdd:PRK11706 219 QVdkytwvdiGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALaplaEAGRIELPSIPDDCKHNAHMFYIKLRD 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169811288 322 LHSRDKLLKLTNDSGVMTR----PvwqlMHRLPMFKDALR--GSLQHSEWFEERLVNLP 374
Cdd:PRK11706 299 LEDRSALINFLKEAGIMAVfhyiP----LHSSPAGERFGRfhGEDRYTTKESERLLRLP 353
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
15-377 1.08e-42

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 152.87  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  15 NEFIPLHAPTFAGNEQAYVAETITSTFVSSvGKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQS 94
Cdd:PRK11658   2 SDFLPFSRPAMGDEELAAVKEVLRSGWITT-GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  95 LTFVATCNALYHMGAAPIFVDISTVSLGLSPQAVQTYLeeygllneeglcihkeTKQTiKAVMPMHTFGHPVELDELVLI 174
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAI----------------TPRT-KAIIPVHYAGAPADLDAIRAI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 175 CQQWNLVLIEDAAESLGSRYKEKHTGTIGEfAALSFNGNKIITTGGGGVLLTNNQ--ANGIR----------AKHITTTA 242
Cdd:PRK11658 144 GERYGIPVIEDAAHAVGTYYKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDelADRLRslkfhglgvdAFDRQTQG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 243 KVPHPYEFyhdEAGFNYRMPNLNAALGCAQMESLPLFIEQKRALAMHYNSFFDGGELLFVQEPSYAKSNYW------LNA 316
Cdd:PRK11658 223 RAPQAEVL---TPGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWhlfiirVDE 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169811288 317 VICPnlHSRDKLLKLTNDSGVMTRPVWQLMH-------RLPMFkdalrgSLQHSEWFEERLVNLPSSP 377
Cdd:PRK11658 300 ERCG--ISRDALMEALKERGIGTGLHFRAAHtqkyyreRFPTL------SLPNTEWNSERICSLPLFP 359
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
46-285 1.77e-34

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 131.93  E-value: 1.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  46 GKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALyMA---------GVQSGDLVITQSLTFVATCNALYHMGAAPIFVDi 116
Cdd:PRK15407  62 GRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAF-SAltspklgdrALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVD- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 117 stVSLGlspqavqTYLEEYGLLnEEGLcihkeTKQTiKAVMPMHTFGHPVELDELVLICQQWNLVLIEDAAESLGSRYKE 196
Cdd:PRK15407 140 --VELP-------TYNIDASLL-EAAV-----SPKT-KAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDG 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 197 KHTGTIGEFAALSFNGNKIITTGGGGVLLTNN-----QANGIR--------AKHITTT---------AKVP----HPYEF 250
Cdd:PRK15407 204 RMTGTFGDIATLSFYPAHHITMGEGGAVFTNDpllkkIIESFRdwgrdcwcAPGCDNTcgkrfgwqlGELPfgydHKYTY 283
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 169811288 251 YHdeAGFNYRMPNLNAALGCAQMESLPLFIEQKRA 285
Cdd:PRK15407 284 SH--LGYNLKITDMQAAIGLAQLEKLPGFIEARKA 316
PRK06234 PRK06234
methionine gamma-lyase; Provisional
12-133 3.11e-05

methionine gamma-lyase; Provisional


Pssm-ID: 168478 [Multi-domain]  Cd Length: 400  Bit Score: 45.59  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  12 YQTNEFIPLHAPT----FAGNEQAYVAETITStfvssvgKFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAgVQSG 87
Cdd:PRK06234  32 YQTSTFIFDSAEQggrrFAGEESGYIYSRLGN-------PTSTEVENKLALLEGGEAAVVAASGMGAISSSLWSA-LKAG 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169811288  88 DLVITQSL----TFVATCNALYHMGAAPIFVDIST---VSLGLSPQAVQTYLE 133
Cdd:PRK06234 104 DHVVASDTlygcTFALLNHGLTRYGVEVTFVDTSNleeVRNALKANTKVVYLE 156
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
48-227 7.83e-05

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: 42.75  E-value: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  48 FVTDFEQKIEAFTQS--PKAIATSSGSSALHTALyMAGVQSGDLVITQSLTFVATcnalYHMGAAPIFVDISTVslglsp 125
Cdd:cd01494    1 KLEELEEKLARLLQPgnDKAVFVPSGTGANEAAL-LALLGPGDEVIVDANGHGSR----YWVAAELAGAKPVPV------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288 126 qavqTYLEEYGLLNEEGLCIHKETKQTIKAVMPMHTFGHP---VELDELVLICQQWNLVLIEDAAESLGSRYKEKHTGTI 202
Cdd:cd01494   70 ----PVDDAGYGGLDVAILEELKAKPNVALIVITPNTTSGgvlVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE 145
                        170       180
                 ....*....|....*....|....*
gi 169811288 203 GEFAALSFNGNKIITTGGGGVLLTN 227
Cdd:cd01494  146 GGADVVTFSLHKNLGGEGGGVVIVK 170
PRK08133 PRK08133
O-succinylhomoserine sulfhydrylase; Validated
22-100 1.50e-03

O-succinylhomoserine sulfhydrylase; Validated


Pssm-ID: 181244 [Multi-domain]  Cd Length: 390  Bit Score: 40.37  E-value: 1.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169811288  22 APTFAGNEQAYvaetITSTFVSSVgkfVTDFEQKIEAFTQSPKAIATSSGSSALhTALYMAGVQSGDLVITQSLTFVAT 100
Cdd:PRK08133  43 AARFAGEEPGN----IYSRFTNPT---VTMFQERLAALEGAEACVATASGMAAI-LAVVMALLQAGDHVVSSRSLFGST 113
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
47-187 3.98e-03

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: 38.86  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169811288  47 KFVTDFEQKIEAFTQSPKAIATSSGSSALHTALYMAGVQSGDLVITQSLTFVATCNALYHMGAAPIFVDistvslglspq 126
Cdd:cd00609   43 EAIAEWLGRRGGVDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVP----------- 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169811288 127 avqtyLEEYGLLNEEGLCIHKETKQTIKAVMpMHTFGHPV-------ELDELVLICQQWNLVLIEDAA 187
Cdd:cd00609  112 -----LDEEGGFLLDLELLEAAKTPKTKLLY-LNNPNNPTgavlseeELEELAELAKKHGILIISDEA 173
 
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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