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Conserved domains on  [gi|489059529|ref|WP_002969594|]
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MULTISPECIES: DegT/DnrJ/EryC1/StrS aminotransferase family protein [Brucella]

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

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];
10-369 2.49e-165

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 466.47  E-value: 2.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  10 RARIENRLNAAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAE 89
Cdd:COG0399    6 RPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATAN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  90 VVALVGAEPVFVDVDPDSYNMNVEQLEAAIAAtikegrlEPKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGG 169
Cdd:COG0399   86 AILYVGATPVFVDIDPDTYNIDPEALEAAITP-------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 170 KRDNVMCGAFGHVGATSFYPAKPLGCyGDGGAMFTNDAELADTLRSVLFHGKG-ETQYDNVRIGINSRLDTIQAAVLLEK 248
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDrDAKYEHVELGYNYRMDELQAAIGLAQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 249 LAILEDEMEARDRIARRYNEALKDV--VKVPELPAGNRSAWAQYSI---ESENRDGLKAQLQAEGIPSVIYYVKPLHLQT 323
Cdd:COG0399  238 LKRLDEFIARRRAIAARYREALADLpgLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQP 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489059529 324 AYKHYSVAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIRGF 369
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];
10-369 2.49e-165

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 466.47  E-value: 2.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  10 RARIENRLNAAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAE 89
Cdd:COG0399    6 RPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATAN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  90 VVALVGAEPVFVDVDPDSYNMNVEQLEAAIAAtikegrlEPKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGG 169
Cdd:COG0399   86 AILYVGATPVFVDIDPDTYNIDPEALEAAITP-------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 170 KRDNVMCGAFGHVGATSFYPAKPLGCyGDGGAMFTNDAELADTLRSVLFHGKG-ETQYDNVRIGINSRLDTIQAAVLLEK 248
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDrDAKYEHVELGYNYRMDELQAAIGLAQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 249 LAILEDEMEARDRIARRYNEALKDV--VKVPELPAGNRSAWAQYSI---ESENRDGLKAQLQAEGIPSVIYYVKPLHLQT 323
Cdd:COG0399  238 LKRLDEFIARRRAIAARYREALADLpgLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQP 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489059529 324 AYKHYSVAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIRGF 369
Cdd:COG0399  318 AYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
19-367 3.84e-143

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: 410.01  E-value: 3.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  19 AAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEP 98
Cdd:cd00616    3 EAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  99 VFVDVDPDSYNMNVEQLEAAIaaTIKegrlePKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRDNVMCGA 178
Cdd:cd00616   83 VFVDIDPDTYNIDPELIEAAI--TPR-----TKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 179 FGHVGATSFYPAKPLgCYGDGGAMFTNDAELADTLRSVLFHGKGET--QYDNVRIGINSRLDTIQAAVLLEKLAILEDEM 256
Cdd:cd00616  156 FGDAGAFSFHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDrfKYEHEILGYNYRLSEIQAAIGLAQLEKLDEII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 257 EARDRIARRYNEALKDV--VKVPELPAGNRSAWAQYSI-----ESENRDGLKAQLQAEGIPSVIYYVKPLHLQTAYKHYS 329
Cdd:cd00616  235 ARRREIAERYKELLADLpgIRLPDVPPGVKHSYHLYVIrldpeAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLG 314
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 489059529 330 VAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIR 367
Cdd:cd00616  315 YPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
13-367 4.42e-119

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: 348.89  E-value: 4.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529   13 IENRLNAAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVA 92
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529   93 LVGAEPVFVDVDPDSYNMNVEQLEAAIaatikEGRlePKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRD 172
Cdd:pfam01041  83 RLGAKPVFVDIDPDTYNIDPEAIEAAI-----TPR--TKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  173 NVMCGAFGHVGATSFYPAKPLgCYGDGGAMFTNDAELADTLRSVLFHG---KGETQYDNVRIGINSRLDTIQAAVLLEKL 249
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGmvrKADKRYWHEVLGYNYRMTEIQAAIGLAQL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  250 AILEDEMEARDRIARRYNEALKDV--VKVPELPAG-NRSAWAQYSI----ESENRDGLKAQLQAEGIPSVIYYVKPLHLQ 322
Cdd:pfam01041 235 ERLDEFIARRREIAALYQTLLADLpgFTPLTTPPEaDVHAWHLFPIlvpeEAINRDELVEALKEAGIGTRVHYPIPLHLQ 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 489059529  323 TAYKH-YSVAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIR 367
Cdd:pfam01041 315 PYYRDlFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
43-369 4.03e-66

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 213.93  E-value: 4.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  43 LGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPDSYNMNVEQLEAAIaaT 122
Cdd:PRK11706  40 LEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAI--T 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 123 IKEgrlepKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRDNVMCGAFGHVGATSFYPAKPLGCyGDGGAM 202
Cdd:PRK11706 118 PKT-----RAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGAL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 203 FTNDAELAD---------TLRSVLFhgKGET-QYDNVRIGiNSRLDT-IQAAVLLEKLAILEDEMEARDRIARRYNEALK 271
Cdd:PRK11706 192 LINDPALIEraeiirekgTNRSQFF--RGQVdKYTWVDIG-SSYLPSeLQAAYLWAQLEAADRINQRRLALWQRYYDALA 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 272 D-----VVKVPELPAGNRSAWAQYSI---ESENRDGLKAQLQAEGIPSVIYYVkPLHLQTAYKHYSVAPGGLPVSESLPS 343
Cdd:PRK11706 269 PlaeagRIELPSIPDDCKHNAHMFYIklrDLEDRSALINFLKEAGIMAVFHYI-PLHSSPAGERFGRFHGEDRYTTKESE 347
                        330       340
                 ....*....|....*....|....*.
gi 489059529 344 RILSLPMHPYLSEADQDKIIGVIRGF 369
Cdd:PRK11706 348 RLLRLPLFYNLTDVEQRTVIDTILEF 373
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
10-369 2.49e-165

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 466.47  E-value: 2.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  10 RARIENRLNAAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAE 89
Cdd:COG0399    6 RPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATAN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  90 VVALVGAEPVFVDVDPDSYNMNVEQLEAAIAAtikegrlEPKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGG 169
Cdd:COG0399   86 AILYVGATPVFVDIDPDTYNIDPEALEAAITP-------RTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 170 KRDNVMCGAFGHVGATSFYPAKPLGCyGDGGAMFTNDAELADTLRSVLFHGKG-ETQYDNVRIGINSRLDTIQAAVLLEK 248
Cdd:COG0399  159 TYKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDrDAKYEHVELGYNYRMDELQAAIGLAQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 249 LAILEDEMEARDRIARRYNEALKDV--VKVPELPAGNRSAWAQYSI---ESENRDGLKAQLQAEGIPSVIYYVKPLHLQT 323
Cdd:COG0399  238 LKRLDEFIARRRAIAARYREALADLpgLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQP 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 489059529 324 AYKHYSVAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIRGF 369
Cdd:COG0399  318 AYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREF 363
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
19-367 3.84e-143

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: 410.01  E-value: 3.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  19 AAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEP 98
Cdd:cd00616    3 EAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  99 VFVDVDPDSYNMNVEQLEAAIaaTIKegrlePKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRDNVMCGA 178
Cdd:cd00616   83 VFVDIDPDTYNIDPELIEAAI--TPR-----TKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 179 FGHVGATSFYPAKPLgCYGDGGAMFTNDAELADTLRSVLFHGKGET--QYDNVRIGINSRLDTIQAAVLLEKLAILEDEM 256
Cdd:cd00616  156 FGDAGAFSFHPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDrfKYEHEILGYNYRLSEIQAAIGLAQLEKLDEII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 257 EARDRIARRYNEALKDV--VKVPELPAGNRSAWAQYSI-----ESENRDGLKAQLQAEGIPSVIYYVKPLHLQTAYKHYS 329
Cdd:cd00616  235 ARRREIAERYKELLADLpgIRLPDVPPGVKHSYHLYVIrldpeAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLG 314
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 489059529 330 VAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIR 367
Cdd:cd00616  315 YPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
13-367 4.42e-119

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: 348.89  E-value: 4.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529   13 IENRLNAAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVA 92
Cdd:pfam01041   3 IDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529   93 LVGAEPVFVDVDPDSYNMNVEQLEAAIaatikEGRlePKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRD 172
Cdd:pfam01041  83 RLGAKPVFVDIDPDTYNIDPEAIEAAI-----TPR--TKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  173 NVMCGAFGHVGATSFYPAKPLgCYGDGGAMFTNDAELADTLRSVLFHG---KGETQYDNVRIGINSRLDTIQAAVLLEKL 249
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGmvrKADKRYWHEVLGYNYRMTEIQAAIGLAQL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  250 AILEDEMEARDRIARRYNEALKDV--VKVPELPAG-NRSAWAQYSI----ESENRDGLKAQLQAEGIPSVIYYVKPLHLQ 322
Cdd:pfam01041 235 ERLDEFIARRREIAALYQTLLADLpgFTPLTTPPEaDVHAWHLFPIlvpeEAINRDELVEALKEAGIGTRVHYPIPLHLQ 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 489059529  323 TAYKH-YSVAPGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIR 367
Cdd:pfam01041 315 PYYRDlFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
43-369 4.03e-66

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 213.93  E-value: 4.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  43 LGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPDSYNMNVEQLEAAIaaT 122
Cdd:PRK11706  40 LEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAI--T 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 123 IKEgrlepKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRDNVMCGAFGHVGATSFYPAKPLGCyGDGGAM 202
Cdd:PRK11706 118 PKT-----RAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGAL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 203 FTNDAELAD---------TLRSVLFhgKGET-QYDNVRIGiNSRLDT-IQAAVLLEKLAILEDEMEARDRIARRYNEALK 271
Cdd:PRK11706 192 LINDPALIEraeiirekgTNRSQFF--RGQVdKYTWVDIG-SSYLPSeLQAAYLWAQLEAADRINQRRLALWQRYYDALA 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 272 D-----VVKVPELPAGNRSAWAQYSI---ESENRDGLKAQLQAEGIPSVIYYVkPLHLQTAYKHYSVAPGGLPVSESLPS 343
Cdd:PRK11706 269 PlaeagRIELPSIPDDCKHNAHMFYIklrDLEDRSALINFLKEAGIMAVFHYI-PLHSSPAGERFGRFHGEDRYTTKESE 347
                        330       340
                 ....*....|....*....|....*.
gi 489059529 344 RILSLPMHPYLSEADQDKIIGVIRGF 369
Cdd:PRK11706 348 RLLRLPLFYNLTDVEQRTVIDTILEF 373
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
19-367 9.36e-59

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 194.86  E-value: 9.36e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  19 AAISKVVAEGRYILGPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEP 98
Cdd:PRK11658  18 AAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  99 VFVDVDPDSYNMNVEQLEAAIAAtikegrlEPKAIIPVDLFGLAASYNRITAIAEREGLFIIEDAAQSIGGKRDNvmcga 178
Cdd:PRK11658  98 VMVDVDRDTLMVTPEAIEAAITP-------RTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKG----- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 179 fGHVGAT-----SFYPAKPLGCyGDGGAMFTNDAELADTLRSVLFHGKGETQYDN-----------VRIGINSRLDTIQA 242
Cdd:PRK11658 166 -RHIGARgtaifSFHAIKNITC-AEGGLVVTDDDELADRLRSLKFHGLGVDAFDRqtqgrapqaevLTPGYKYNLADINA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 243 AVLLEKLAILeDEMEARDR-IARRYNEALKDV----VKVPELPagNRSAWAQYSIESE------NRDGLKAQLQAEGIPS 311
Cdd:PRK11658 244 AIALVQLAKL-EALNARRReIAARYLQALADLpfqpLSLPAWP--HQHAWHLFIIRVDeercgiSRDALMEALKERGIGT 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489059529 312 VIYYvKPLHLQTAYK-HYSVApgGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIR 367
Cdd:PRK11658 321 GLHF-RAAHTQKYYReRFPTL--SLPNTEWNSERICSLPLFPDMTDADVDRVITALQ 374
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
33-374 7.77e-35

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 132.70  E-value: 7.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  33 GPEVAEFEKKLGEYLGVEHVIACANGTDALQMPLMT--------RGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVD 104
Cdd:PRK15407  62 GRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAltspklgdRALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 105 PDSYNMNVEQLEAAIAAtikegrlEPKAII-------PVDLfglaasyNRITAIAEREGLFIIEDAAQSIGGKRDNVMCG 177
Cdd:PRK15407 142 LPTYNIDASLLEAAVSP-------KTKAIMiahtlgnPFDL-------AAVKAFCDKHNLWLIEDNCDALGSTYDGRMTG 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 178 AFGHVGATSFYPAKPLgCYGDGGAMFTNDAELADTLRSvlFH----------GKGET-------Q-------YDN----V 229
Cdd:PRK15407 208 TFGDIATLSFYPAHHI-TMGEGGAVFTNDPLLKKIIES--FRdwgrdcwcapGCDNTcgkrfgwQlgelpfgYDHkytyS 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 230 RIGINSRLDTIQAAVLLEKLAILEDEMEARDRIARRYNEALKDVVKVPELP---AGNRSAWAQYSI----ESE-NRDGLK 301
Cdd:PRK15407 285 HLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASLEDFLILPeatPNSDPSWFGFPItvkeDAGfTRVELV 364
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489059529 302 AQLQAEGIPSVIYYVKPLHLQTAYKH--YSVApGGLPVSESLPSRILSLPMHPYLSEADQDKIIGVIRGFHGKKA 374
Cdd:PRK15407 365 KYLEENKIGTRLLFAGNLTRQPYFKGvkYRVV-GELTNTDRIMNDTFWIGVYPGLTEEMLDYVIEKIEEFFGLNF 438
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
37-266 2.40e-09

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 58.09  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529   37 AEFEKKLGEYLGVEHVIA--------CANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDV-DPDS 107
Cdd:pfam00155  42 PELREALAKFLGRSPVLKldreaavvFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSND 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  108 YNMNVEQLEAAIAAtikegrlEPKAIIPVDLF---GLAAS---YNRITAIAEREGLFIIEDAAQSIGG--------KRDN 173
Cdd:pfam00155 122 FHLDFDALEAALKE-------KPKVVLHTSPHnptGTVATleeLEKLLDLAKEHNILLLVDEAYAGFVfgspdavaTRAL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  174 VMCGAFGHVgATSFypAKPLGCYGDGGAMFTNDAELADTLRSVLFHGKGETQydnvriginsrLDTIQAAVLLEKLAILE 253
Cdd:pfam00155 195 LAEGPNLLV-VGSF--SKAFGLAGWRVGYILGNAAVISQLRKLARPFYSSTH-----------LQAAAAAALSDPLLVAS 260
                         250
                  ....*....|...
gi 489059529  254 DEMEARDRIARRY 266
Cdd:pfam00155 261 ELEEMRQRIKERR 273
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
36-205 2.60e-09

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: 55.85  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  36 VAEFEKKLGEYL--GVEHVIACANGTDALQMPLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPDSYN-MNV 112
Cdd:cd01494    2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGgLDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 113 EQLEAAiaatikEGRLEPKAIIPVDLFGLAASYN---RITAIAEREGLFIIEDAAQSIGGKRDNVMCGAFGHVGATSFYP 189
Cdd:cd01494   82 AILEEL------KAKPNVALIVITPNTTSGGVLVplkEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSL 155
                        170
                 ....*....|....*.
gi 489059529 190 AKPLGCYGdGGAMFTN 205
Cdd:cd01494  156 HKNLGGEG-GGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
35-275 6.47e-07

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: 50.80  E-value: 6.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  35 EVAEF-EKKLGEYLGVEHVIACANGTDALQMpLMTRGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPDSYNMNVE 113
Cdd:cd00609   44 AIAEWlGRRGGVDVPPEEIVVTNGAQEALSL-LLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 114 QLEAAIAATikegrlEPKAII------PVdlfGLAASYNRITAI---AEREGLFIIEDAA-------------QSIGGKR 171
Cdd:cd00609  123 ELLEAAKTP------KTKLLYlnnpnnPT---GAVLSEEELEELaelAKKHGILIISDEAyaelvydgepppaLALLDAY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529 172 DNVMCgafghvgATSFypAKPLGCYG-DGGAMFTNDAELADTLRSVLfhgkgetqyDNVRIGINSrldTIQAAVllekLA 250
Cdd:cd00609  194 ERVIV-------LRSF--SKTFGLPGlRIGYLIAPPEELLERLKKLL---------PYTTSGPST---LSQAAA----AA 248
                        250       260
                 ....*....|....*....|....*
gi 489059529 251 ILEDEMEARDRIARRYNEALKDVVK 275
Cdd:cd00609  249 ALDDGEEHLEELRERYRRRRDALLE 273
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
59-162 3.99e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 45.10  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  59 TDALQMPLMTRgIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPDSYNMNVEQLEAAIAAtiKEGRLepKAII---P 135
Cdd:PRK07309 101 TEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILE--QGDKL--KAVIlnyP 175
                         90       100       110
                 ....*....|....*....|....*....|
gi 489059529 136 VDLFGLAASYNRITAIAE---REGLFIIED 162
Cdd:PRK07309 176 ANPTGVTYSREQIKALADvlkKYDIFVISD 205
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
36-162 4.97e-05

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: 44.74  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  36 VAEFEKKLGEYLGVEHVIACANGTDALQMPLMTrGIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDP-DSYNMNVEQ 114
Cdd:COG0436   77 AAYYKRRYGVDLDPDEILVTNGAKEALALALLA-LLNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEeNGFLPDPEA 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489059529 115 LEAAIAAtikegrlEPKAII------PVdlfglAASYNR-----ITAIAEREGLFIIED 162
Cdd:COG0436  156 LEAAITP-------RTKAIVlnspnnPT-----GAVYSReeleaLAELAREHDLLVISD 202
PRK05764 PRK05764
aspartate aminotransferase; Provisional
50-162 5.86e-05

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 44.73  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059529  50 EHVIACANGTDALQMPLMTRgIGPGHAVFVPSFTFAATAEVVALVGAEPVFVDVDPD-SYNMNVEQLEAAIaaTIKegrl 128
Cdd:PRK05764  92 SQVIVTTGAKQALYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEEnGFKLTVEQLEAAI--TPK---- 164
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489059529 129 ePKAII---PVDLFGLAASYNRITAIAE---REGLFIIED 162
Cdd:PRK05764 165 -TKALIlnsPSNPTGAVYSPEELEAIADvavEHDIWVLSD 203
 
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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