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Conserved domains on  [gi|1084038696|gb|OGK44617|]
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hypothetical protein A2957_00915 [Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_38_11]

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];
1-359 6.51e-155

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 439.50  E-value: 6.51e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:COG0399     9 IGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:COG0399    89 YVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGTF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTwkrqgakkyswQYDVQYVGYKYHTNDILSAIGLVQ 240
Cdd:COG0399   169 GDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-----------KYEHVELGYNYRMDELQAAIGLAQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 241 LGKLPQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIK---TEHRDALSSYLADQKISTTVHYE-PNHFYP 316
Cdd:COG0399   238 LKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRldeGEDRDELIAALKARGIGTRVHYPiPLHLQP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1084038696 317 IYKKYAKK---LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKSF 359
Cdd:COG0399   318 AYRDLGYRpgdLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-359 6.51e-155

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 439.50  E-value: 6.51e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:COG0399     9 IGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:COG0399    89 YVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGTF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTwkrqgakkyswQYDVQYVGYKYHTNDILSAIGLVQ 240
Cdd:COG0399   169 GDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-----------KYEHVELGYNYRMDELQAAIGLAQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 241 LGKLPQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIK---TEHRDALSSYLADQKISTTVHYE-PNHFYP 316
Cdd:COG0399   238 LKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRldeGEDRDELIAALKARGIGTRVHYPiPLHLQP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1084038696 317 IYKKYAKK---LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKSF 359
Cdd:COG0399   318 AYRDLGYRpgdLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 5-357 5.56e-147

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: 419.25  E-value: 5.56e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   5 ETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVILYQKA 84
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  85 TPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTIGDFG 164
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 165 CFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRwmgiskdtwkRQGAKKYSWQYDVQYVGYKYHTNDILSAIGLVQLGKL 244
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLR----------NHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 245 PQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIKT-----EHRDALSSYLADQKISTTVHYEPNHFYPIYK 319
Cdd:cd00616   231 DEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLdpeagESRDELIEALKEAGIETRVHYPPLHHQPPYK 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1084038696 320 KY----AKKLPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVK 357
Cdd:cd00616   311 KLlgypPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 1-357 1.06e-127

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: 370.46  E-value: 1.06e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:pfam01041  83 RLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKkyswqydvqYVGYKYHTNDILSAIGLVQ 240
Cdd:pfam01041 163 GDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHE---------VLGYNYRMTEIQAAIGLAQ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 241 LGKLPQVMKRKWEIFNRYNKAF-SRVNWLKIPVQKSYTTHALHNYCIKTE----HRDALSSYLADQKISTTVHY-EPNHF 314
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLaDLPGFTPLTTPPEADVHAWHLFPILVPeeaiNRDELVEALKEAGIGTRVHYpIPLHL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1084038696 315 YPIYKKYAKK----LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVK 357
Cdd:pfam01041 314 QPYYRDLFGYapgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 12-358 2.16e-97

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: 293.85  E-value: 2.16e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  12 VLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDV 91
Cdd:TIGR03588  19 VLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  92 DPETLCADPKDVIKKITS----KTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI--GDFGC 165
Cdd:TIGR03588  99 DPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCryADATV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 166 FSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKKYSWQYDVQYVGYKYHTNDILSAIGLVQLGKLP 245
Cdd:TIGR03588 179 FSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPWYYEQQELGFNYRMTDIQAALGLSQLKKLD 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 246 QVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNY--CIKTE---HRDALSSYLADQKISTTVHYEPNHFYPIYKK 320
Cdd:TIGR03588 259 RFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYpiLLDQEfgcTRKEVFEALRAAGIGVQVHYIPVHLQPYYRQ 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1084038696 321 YAK--KLPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKS 358
Cdd:TIGR03588 339 GFGdgDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRK 378
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 4-359 4.35e-92

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 280.18  E-value: 4.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   4 QETNEVKGVLESGWI-GLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVST-NHVILy 81
Cdd:PRK11706   12 TELDYIQQAMSSGKLcGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTaNAFVL- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  82 QKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTIG 161
Cdd:PRK11706   91 RGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 162 DFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKKYSWQyDvqyVGYKYHTNDILSAIGLVQL 241
Cdd:PRK11706  171 HIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWV-D---IGSSYLPSELQAAYLWAQL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 242 GKLPQVMKRKWEIFNRYNKAFSRV---NWLKIPVQKSYTTHALHNYCIKT---EHRDALSSYLADQKISTTVHYEPNHFY 315
Cdd:PRK11706  247 EAADRINQRRLALWQRYYDALAPLaeaGRIELPSIPDDCKHNAHMFYIKLrdlEDRSALINFLKEAGIMAVFHYIPLHSS 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1084038696 316 PIYKKYAKK---LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKSF 359
Cdd:PRK11706  327 PAGERFGRFhgeDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-359 6.51e-155

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 439.50  E-value: 6.51e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:COG0399     9 IGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:COG0399    89 YVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGTF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTwkrqgakkyswQYDVQYVGYKYHTNDILSAIGLVQ 240
Cdd:COG0399   169 GDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA-----------KYEHVELGYNYRMDELQAAIGLAQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 241 LGKLPQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIK---TEHRDALSSYLADQKISTTVHYE-PNHFYP 316
Cdd:COG0399   238 LKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRldeGEDRDELIAALKARGIGTRVHYPiPLHLQP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1084038696 317 IYKKYAKK---LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKSF 359
Cdd:COG0399   318 AYRDLGYRpgdLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 5-357 5.56e-147

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: 419.25  E-value: 5.56e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   5 ETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVILYQKA 84
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  85 TPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTIGDFG 164
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 165 CFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRwmgiskdtwkRQGAKKYSWQYDVQYVGYKYHTNDILSAIGLVQLGKL 244
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLR----------NHGRDRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 245 PQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIKT-----EHRDALSSYLADQKISTTVHYEPNHFYPIYK 319
Cdd:cd00616   231 DEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLdpeagESRDELIEALKEAGIETRVHYPPLHHQPPYK 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1084038696 320 KY----AKKLPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVK 357
Cdd:cd00616   311 KLlgypPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 1-357 1.06e-127

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: 370.46  E-value: 1.06e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:pfam01041  83 RLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKkyswqydvqYVGYKYHTNDILSAIGLVQ 240
Cdd:pfam01041 163 GDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHE---------VLGYNYRMTEIQAAIGLAQ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 241 LGKLPQVMKRKWEIFNRYNKAF-SRVNWLKIPVQKSYTTHALHNYCIKTE----HRDALSSYLADQKISTTVHY-EPNHF 314
Cdd:pfam01041 234 LERLDEFIARRREIAALYQTLLaDLPGFTPLTTPPEADVHAWHLFPILVPeeaiNRDELVEALKEAGIGTRVHYpIPLHL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1084038696 315 YPIYKKYAKK----LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVK 357
Cdd:pfam01041 314 QPYYRDLFGYapgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 12-358 2.16e-97

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: 293.85  E-value: 2.16e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  12 VLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDV 91
Cdd:TIGR03588  19 VLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  92 DPETLCADPKDVIKKITS----KTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI--GDFGC 165
Cdd:TIGR03588  99 DPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCryADATV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 166 FSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKKYSWQYDVQYVGYKYHTNDILSAIGLVQLGKLP 245
Cdd:TIGR03588 179 FSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPWYYEQQELGFNYRMTDIQAALGLSQLKKLD 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 246 QVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNY--CIKTE---HRDALSSYLADQKISTTVHYEPNHFYPIYKK 320
Cdd:TIGR03588 259 RFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYpiLLDQEfgcTRKEVFEALRAAGIGVQVHYIPVHLQPYYRQ 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1084038696 321 YAK--KLPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKS 358
Cdd:TIGR03588 339 GFGdgDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRK 378
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 4-359 4.35e-92

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 280.18  E-value: 4.35e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   4 QETNEVKGVLESGWI-GLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVST-NHVILy 81
Cdd:PRK11706   12 TELDYIQQAMSSGKLcGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTaNAFVL- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  82 QKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTIG 161
Cdd:PRK11706   91 RGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 162 DFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQGAKKYSWQyDvqyVGYKYHTNDILSAIGLVQL 241
Cdd:PRK11706  171 HIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWV-D---IGSSYLPSELQAAYLWAQL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 242 GKLPQVMKRKWEIFNRYNKAFSRV---NWLKIPVQKSYTTHALHNYCIKT---EHRDALSSYLADQKISTTVHYEPNHFY 315
Cdd:PRK11706  247 EAADRINQRRLALWQRYYDALAPLaeaGRIELPSIPDDCKHNAHMFYIKLrdlEDRSALINFLKEAGIMAVFHYIPLHSS 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1084038696 316 PIYKKYAKK---LPVTEKLYNEILLLPFYYGLSDQEIDYIIEKVKSF 359
Cdd:PRK11706  327 PAGERFGRFhgeDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEF 373
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-353 2.86e-88

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 270.74  E-value: 2.86e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQETNEVKGVLESGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALIVAGVTEGDEVISPSLTFVSTNHVIL 80
Cdd:PRK11658   12 MGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  81 YQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTI 160
Cdd:PRK11658   92 LLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGAR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 161 GDfGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYRWMGISKDTWKRQ--GAKKyswQYDVQYVGYKYHTNDILSAIGL 238
Cdd:PRK11658  172 GT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQtqGRAP---QAEVLTPGYKYNLADINAAIAL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 239 VQLGKLPQVMKRKWEIFNRYNKAFSRVNWLKIPVQKSYTTHALHNYCIKTEH------RDALSSYLADQKISTTVHYEPN 312
Cdd:PRK11658  248 VQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEercgisRDALMEALKERGIGTGLHFRAA 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1084038696 313 HFYPIYKKY--AKKLPVTEKLYNEILLLPFYYGLSDQEIDYII 353
Cdd:PRK11658  328 HTQKYYRERfpTLSLPNTEWNSERICSLPLFPDMTDADVDRVI 370
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 1-359 8.51e-53

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 180.46  E-value: 8.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696   1 MDAQE-TNEVKGVLEsGWIGLGPKTEEFEKALEVYLGNKHIITTNSATAALHLALivAGVT----------EGDEVISPS 69
Cdd:PRK15407   42 IDAKElQNLVDASLD-FWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAF--SALTspklgdralkPGDEVITVA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  70 LTFVSTNHVILYQKATPVFCDVDPETLCADPKDVIKKITSKTKAIIVVHYGGHAVDMDPILMAARKKNIMVIEDAAHALG 149
Cdd:PRK15407  119 AGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 150 GKYKGKMLGTIGDFGCFSFHAVKAVAMGDGGAIFTKSKKTAAMLKAYR-WmgiSKDTWKRQG-----AKKYSWQ------ 217
Cdd:PRK15407  199 STYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRdW---GRDCWCAPGcdntcGKRFGWQlgelpf 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 218 -YDVQYV----GYKYHTNDILSAIGLVQLGKLPQ-VMKRKwEIFNRYNKAF---------------SRVNWLKIPVQksy 276
Cdd:PRK15407  276 gYDHKYTyshlGYNLKITDMQAAIGLAQLEKLPGfIEARK-ANFAYLKEGLasledflilpeatpnSDPSWFGFPIT--- 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 277 tthalhnycIKTEH---RDALSSYLADQKISTTVHYEPN---HFYPIYKKY--AKKLPVTEKLYNEILLLPFYYGLSDQE 348
Cdd:PRK15407  352 ---------VKEDAgftRVELVKYLEENKIGTRLLFAGNltrQPYFKGVKYrvVGELTNTDRIMNDTFWIGVYPGLTEEM 422

                         410
                  ....*....|.
gi 1084038696 349 IDYIIEKVKSF 359
Cdd:PRK15407  423 LDYVIEKIEEF 433
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 33-147 2.02e-11

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 64.28  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  33 VYLGNKHIITTNSATAALHLALIVAgVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPE-TLCADPKDVIKKITSKT 111
Cdd:cd00609    55 VDVPPEEIVVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKT 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084038696 112 KAIIVVHYG---GHAVDMD---PILMAARKKNIMVIEDAAHA 147
Cdd:cd00609   134 KLLYLNNPNnptGAVLSEEeleELAELAKKHGILIISDEAYA 175
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 25-185 3.34e-11

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: 61.24  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  25 EEFEK-ALEVYL-GNKHIITTNSATAALHlALIVAGVTEGDEVISPSLTFVS-TNHVILYQKATPVFCDVDPETLC-ADP 100
Cdd:cd01494     3 EELEEkLARLLQpGNDKAVFVPSGTGANE-AALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGgLDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696 101 KDVIKKITSKTKAIIVVHYGGH----AVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTIG--DFGCFSFHavKAV 174
Cdd:cd01494    82 AILEELKAKPNVALIVITPNTTsggvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGgaDVVTFSLH--KNL 159

                         170
                  ....*....|.
gi 1084038696 175 AMGDGGAIFTK 185
Cdd:cd01494   160 GGEGGGVVIVK 170
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 39-143 3.66e-10

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: 60.91  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  39 HIITTNSATAALHLALiVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPET-LCADPKDVIKKITSKTKAIIVV 117
Cdd:COG0436    92 EILVTNGAKEALALAL-LALLNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEALEAAITPRTKAIVLN 170

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1084038696 118 HYG---GhAV----DMDPILMAARKKNIMVIED 143
Cdd:COG0436   171 SPNnptG-AVysreELEALAELAREHDLLVISD 202
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 38-116 6.65e-07

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 50.51  E-value: 6.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  38 KHIITTNSATAALHLALIVAgVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPET-LCADPKDVIKKITSKTKAIIV 116
Cdd:PRK05764   92 SQVIVTTGAKQALYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIL 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-150 2.19e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.84  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  26 EFEKALEVYLGNKH---------IITTNSATAALhLALIVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDV-DPET 95
Cdd:pfam00155  43 ELREALAKFLGRSPvlkldreaaVVFGSGAGANI-EALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSND 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084038696  96 LCADPKDVIKKITSKTKaiIVVHYGGHA---VDMDP-----ILMAARKKNIMVIEDAAHALGG 150
Cdd:pfam00155 122 FHLDFDALEAALKEKPK--VVLHTSPHNptgTVATLeelekLLDLAKEHNILLLVDEAYAGFV 182
PRK08363 PRK08363
alanine aminotransferase; Validated
 38-117 4.01e-06

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 48.27  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  38 KHIITTNSATAALHLaLIVAGVTEGDEVISPSLTF-VSTNHVILYQkATPVFCD-VDPETLCADPKDVIKKITSKTKAII 115
Cdd:PRK08363   94 DDVRVTAAVTEALQL-IFGALLDPGDEILIPGPSYpPYTGLVKFYG-GVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIA 171


                  ..
gi 1084038696 116 VV 117
Cdd:PRK08363  172 VI 173
PRK07682 PRK07682
aminotransferase;
34-147 4.27e-06

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 48.19  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  34 YLGNKHIITTNSATAALHLALiVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPET-LCADPKDVIKKITSKTK 112
Cdd:PRK07682   78 YDPNDEIIVTVGASQALDVAM-RAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTK 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1084038696 113 AIIVVHYGG------HAVDMDPILMAARKKNIMVIEDAAHA 147
Cdd:PRK07682  157 AILLCSPNNptgavlNKSELEEIAVIVEKHDLIVLSDEIYA 197
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
24-149 5.08e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 47.83  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  24 TEEFEKALEV---YLG---NKHIITTNSATAALHL-ALIVAGVTEGDEVISPSLTFVStNHVILYQ-----KATPVFCDV 91
Cdd:COG0520    58 TDAYEAAREKvarFIGaasPDEIIFTRGTTEAINLvAYGLGRLKPGDEILITEMEHHS-NIVPWQElaertGAEVRVIPL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084038696  92 DpETLCADPKDVIKKITSKTKAIIVVH---YGGHAVDMDPILMAARKKNIMVIEDAAHALG 149
Cdd:COG0520   137 D-EDGELDLEALEALLTPRTKLVAVTHvsnVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
PRK12414 PRK12414
putative aminotransferase; Provisional
 34-116 3.42e-05

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 45.16  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  34 YLGNKHIITTNSATAALHLAlIVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPETLCADPKDVIKKITSKTKA 113
Cdd:PRK12414   87 YDPASEVTVIASASEGLYAA-ISALVHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRM 165


                  ...
gi 1084038696 114 IIV 116
Cdd:PRK12414  166 IIV 168
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
39-116 3.59e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 45.18  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  39 HIITTNSATAALHLALiVAGVTEGDEVISPSLTFV-----STNHvilyqKATPVFCDVDPETLCADPKDVIKKITSKTKA 113
Cdd:PRK06836   98 HIVMTCGAAGALNVAL-KAILNPGDEVIVFAPYFVeyrfyVDNH-----GGKLVVVPTDTDTFQPDLDALEAAITPKTKA 171


                  ...
gi 1084038696 114 IIV 116
Cdd:PRK06836  172 VII 174
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 21-183 5.79e-05

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


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 44.16  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  21 GPKTEEFEKALEVYlGNKH-IITTNSATAALhLALIVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFC--DVDPET-- 95
Cdd:cd00615    59 GPIKEAQELAARAF-GAKHtFFLVNGTSSSN-KAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLkpERNPYYgi 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  96 -LCADPKDVIKKITSKT--KAIIVVH--YGGHAVDMDPILMAARKKNIMVIEDAAHalggkykgkmlgtigdFGCFSFHA 170
Cdd:cd00615   137 aGGIPPETFKKALIEHPdaKAAVITNptYYGICYNLRKIVEEAHHRGLPVLVDEAH----------------GAHFRFHP 200

                         170
                  ....*....|...
gi 1084038696 171 VKAVAMGDGGAIF 183
Cdd:cd00615   201 ILPSSAAMAGADI 213
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
27-116 1.64e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 43.17  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  27 FEKALEVYLGNKHIITTNSATAALHLALiVAGVTEGDEVISPSLTFVSTNHVILYQKATPVFCD-VDPETLCADPKDVIK 105
Cdd:PRK06348   79 YSKNYDLSFKRNEIMATVGACHGMYLAL-QSILDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEA 157

                          90
                  ....*....|.
gi 1084038696 106 KITSKTKAIIV 116
Cdd:PRK06348  158 LITSKTKAIIL 168
PRK07683 PRK07683
aminotransferase A; Validated
 34-143 1.79e-04

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 43.17  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  34 YLGNKHIITTNSATAALHLALIVAgVTEGDEVISPSLTFVSTNHVILYQKATPVFCDVDPETLCADPKDVIKKITSKTKA 113
Cdd:PRK07683   86 YSPESEIIVTIGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRC 164

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1084038696 114 IIVVHYG---GHAVD---MDPILMAARKKNIMVIED 143
Cdd:PRK07683  165 VVLPYPSnptGVTLSkeeLQDIADVLKDKNIFVLSD 200
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 22-197 1.76e-03

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


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 39.88  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  22 PKTEEFEKALEVYLGNKHIITTNSATAALHLALiVAGVTEGDEVISPSLTFVSTNhvILYQKATPVFC----DVDPetlc 97
Cdd:cd00614    40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVL-LALLKAGDHVVASDDLYGGTY--RLFERLLPKLGievtFVDP---- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038696  98 ADPKDVIKKITSKTKAIIV---VHYGGHAVDMDPILMAARKKNIMVIEDAAHALGGKYKGKMLGTigDFGCFSfhAVKAV 174
Cdd:cd00614   113 DDPEALEAAIKPETKLVYVespTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQRPLELGA--DIVVHS--ATKYI 188

                         170       180
                  ....*....|....*....|....*.
gi 1084038696 175 A-MGD--GGAIFTKSKKTAAMLKAYR 197
Cdd:cd00614   189 GgHSDviAGVVVGSGEALIQRLRFLR 214
 
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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