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Conserved domains on  [gi|489175677|ref|WP_003085203|]
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MULTISPECIES: anthranilate phosphoribosyltransferase [Pseudomonas]

Protein Classification

anthranilate phosphoribosyltransferase( domain architecture ID 11478311)

anthranilate phosphoribosyltransferase catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA)

Gene Ontology:  GO:0004048|GO:0000162|GO:0046872
PubMed:  36633281|28844746
SCOP:  4003843|4000984

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
trpD PRK00188
anthranilate phosphoribosyltransferase; Provisional
1-340 4.69e-175

anthranilate phosphoribosyltransferase; Provisional


:

Pssm-ID: 234682 [Multi-domain]  Cd Length: 339  Bit Score: 489.20  E-value: 4.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   1 MDIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELAdgVQLPTLKHVVDV 80
Cdd:PRK00188   1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHA--VPVPDPDDAVDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  81 VGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKA 160
Cdd:PRK00188  79 VGTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 161 MKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAEL 240
Cdd:PRK00188 159 MKHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHGSDGLDEISLTGPTTVAEL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 241 KDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAgqkAAELIVMNAGPALYAADLATSLHEGIQLA 320
Cdd:PRK00188 239 KDGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGA---ARDAVLLNAAAALYVAGKADDLKEGVELA 315
                        330       340
                 ....*....|....*....|
gi 489175677 321 HDALHTGLAREKMDELVAFT 340
Cdd:PRK00188 316 REAIDSGAALAKLEELVAFS 335
 
Name Accession Description Interval E-value
trpD PRK00188
anthranilate phosphoribosyltransferase; Provisional
1-340 4.69e-175

anthranilate phosphoribosyltransferase; Provisional


Pssm-ID: 234682 [Multi-domain]  Cd Length: 339  Bit Score: 489.20  E-value: 4.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   1 MDIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELAdgVQLPTLKHVVDV 80
Cdd:PRK00188   1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHA--VPVPDPDDAVDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  81 VGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKA 160
Cdd:PRK00188  79 VGTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 161 MKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAEL 240
Cdd:PRK00188 159 MKHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHGSDGLDEISLTGPTTVAEL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 241 KDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAgqkAAELIVMNAGPALYAADLATSLHEGIQLA 320
Cdd:PRK00188 239 KDGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGA---ARDAVLLNAAAALYVAGKADDLKEGVELA 315
                        330       340
                 ....*....|....*....|
gi 489175677 321 HDALHTGLAREKMDELVAFT 340
Cdd:PRK00188 316 REAIDSGAALAKLEELVAFS 335
TrpD COG0547
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ...
2-333 5.87e-153

Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]; Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440313 [Multi-domain]  Cd Length: 327  Bit Score: 432.58  E-value: 5.87e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   2 DIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTlKHVVDVV 81
Cdd:COG0547    1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPD-GDVVDIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  82 GTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAM 161
Cdd:COG0547   80 GTGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEAGIGFLFAPLFHPAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 162 KYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAELK 241
Cdd:COG0547  160 KHVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLLGVKRALVVHGLDGLDEISLTGPTKVAELR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 242 DGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALgrrkteAGQK--AAELIVMNAGPALYAADLATSLHEGIQL 319
Cdd:COG0547  240 DGEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVL------AGEGgpARDAVLLNAAAALYVAGKADSLAEGVEL 313
                        330
                 ....*....|....
gi 489175677 320 AHDALHTGLAREKM 333
Cdd:COG0547  314 AREAIDSGAALAKL 327
trpD TIGR01245
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ...
7-339 1.88e-134

anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27) [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273522 [Multi-domain]  Cd Length: 330  Bit Score: 385.85  E-value: 1.88e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677    7 LNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLKHVVDVVGTGGD 86
Cdd:TIGR01245   1 LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPGRPPEDLVDIVGTGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   87 GANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAMKYAAG 166
Cdd:TIGR01245  81 GANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEETGIGFLFAPLYHPAMKHVAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  167 PRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAELKDGEVR 246
Cdd:TIGR01245 161 VRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKRALVVHGDDGLDEISLTGPTTVAELKDGEIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  247 EYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAgqkAAELIVMNAGPALYAADLATSLHEGIQLAHDALHT 326
Cdd:TIGR01245 241 EYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGSGA---KRDIVALNAAAALYVAGRASDLKEGVELALEAIDS 317
                         330
                  ....*....|...
gi 489175677  327 GLAREKMDELVAF 339
Cdd:TIGR01245 318 GAAAEKLEELVAF 330
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
74-330 2.97e-113

Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.


Pssm-ID: 459860 [Multi-domain]  Cd Length: 253  Bit Score: 329.25  E-value: 2.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   74 LKHVVDVVGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMF 153
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNTFNISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEALGINLDLTPEQVRKLLDEVGVGFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  154 AQVHHKAMKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSrDGLDEFSLAA 233
Cdd:pfam00591  81 APNYHPAMKHVAPVRRELGIRTVFNLLGPLINPARVKRQVLGVYSKELAEGLAEVLKDLGRERAAVVHG-DGLDEASLLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  234 ATHIAELKDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAGqkaAELIVMNAGPALYAADLATSL 313
Cdd:pfam00591 160 KTTVAELKDGEITEYTLTPEDFGLGRATLEALEGGSPKENADILKGVLGGKGSAAH---RDLVALNAGAALYLAGKADSL 236
                         250
                  ....*....|....*..
gi 489175677  314 HEGIQLAHDALHTGLAR 330
Cdd:pfam00591 237 KEGVAKALEVIDSGKAL 253
 
Name Accession Description Interval E-value
trpD PRK00188
anthranilate phosphoribosyltransferase; Provisional
1-340 4.69e-175

anthranilate phosphoribosyltransferase; Provisional


Pssm-ID: 234682 [Multi-domain]  Cd Length: 339  Bit Score: 489.20  E-value: 4.69e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   1 MDIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELAdgVQLPTLKHVVDV 80
Cdd:PRK00188   1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHA--VPVPDPDDAVDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  81 VGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKA 160
Cdd:PRK00188  79 VGTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 161 MKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAEL 240
Cdd:PRK00188 159 MKHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHGSDGLDEISLTGPTTVAEL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 241 KDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAgqkAAELIVMNAGPALYAADLATSLHEGIQLA 320
Cdd:PRK00188 239 KDGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGA---ARDAVLLNAAAALYVAGKADDLKEGVELA 315
                        330       340
                 ....*....|....*....|
gi 489175677 321 HDALHTGLAREKMDELVAFT 340
Cdd:PRK00188 316 REAIDSGAALAKLEELVAFS 335
TrpD COG0547
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ...
2-333 5.87e-153

Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]; Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440313 [Multi-domain]  Cd Length: 327  Bit Score: 432.58  E-value: 5.87e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   2 DIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTlKHVVDVV 81
Cdd:COG0547    1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPD-GDVVDIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  82 GTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAM 161
Cdd:COG0547   80 GTGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEAGIGFLFAPLFHPAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 162 KYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAELK 241
Cdd:COG0547  160 KHVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLLGVKRALVVHGLDGLDEISLTGPTKVAELR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 242 DGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALgrrkteAGQK--AAELIVMNAGPALYAADLATSLHEGIQL 319
Cdd:COG0547  240 DGEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVL------AGEGgpARDAVLLNAAAALYVAGKADSLAEGVEL 313
                        330
                 ....*....|....
gi 489175677 320 AHDALHTGLAREKM 333
Cdd:COG0547  314 AREAIDSGAALAKL 327
trpD TIGR01245
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ...
7-339 1.88e-134

anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27) [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273522 [Multi-domain]  Cd Length: 330  Bit Score: 385.85  E-value: 1.88e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677    7 LNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLKHVVDVVGTGGD 86
Cdd:TIGR01245   1 LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPGRPPEDLVDIVGTGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   87 GANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAMKYAAG 166
Cdd:TIGR01245  81 GANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEETGIGFLFAPLYHPAMKHVAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  167 PRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAELKDGEVR 246
Cdd:TIGR01245 161 VRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKRALVVHGDDGLDEISLTGPTTVAELKDGEIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  247 EYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAgqkAAELIVMNAGPALYAADLATSLHEGIQLAHDALHT 326
Cdd:TIGR01245 241 EYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGSGA---KRDIVALNAAAALYVAGRASDLKEGVELALEAIDS 317
                         330
                  ....*....|...
gi 489175677  327 GLAREKMDELVAF 339
Cdd:TIGR01245 318 GAAAEKLEELVAF 330
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
2-341 2.60e-117

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 349.79  E-value: 2.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   2 DIKGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTlKHVVDVV 81
Cdd:PRK14607 194 DIKSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELAGFASVMREKSRHIPAPS-PRTVDTC 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  82 GTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAM 161
Cdd:PRK14607 273 GTGGDGFGTFNISTTSAFVVAAAGVPVAKHGNRAVSSKSGSADVLEALGVKLEMTPEEAASVLRETGFSFLFAPLFHPAM 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 162 KYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIAELK 241
Cdd:PRK14607 353 KHAAPARRELGIRTAFNLLGPLTNPARVKYQIVGVFDPSYAEPLAQALQRLGTERAMVVSGIDGYDEISTCGPTQILELE 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 242 DGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALgrrKTEAGQKAAELIVMNAGPALYAADLATSLHEGIQLAH 321
Cdd:PRK14607 433 DGEIVTYTFDPEELGLKRVDPEELKGGDPQENYRLAEDVL---KGEPRRPQRDAVALNAGAALYLVGEADSIKEGVGKAL 509
                        330       340
                 ....*....|....*....|
gi 489175677 322 DALHTGLAREKMDELVAFTA 341
Cdd:PRK14607 510 DLIDDGRAYKKLEEVMDLSK 529
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
74-330 2.97e-113

Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.


Pssm-ID: 459860 [Multi-domain]  Cd Length: 253  Bit Score: 329.25  E-value: 2.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   74 LKHVVDVVGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMF 153
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNTFNISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEALGINLDLTPEQVRKLLDEVGVGFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  154 AQVHHKAMKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSrDGLDEFSLAA 233
Cdd:pfam00591  81 APNYHPAMKHVAPVRRELGIRTVFNLLGPLINPARVKRQVLGVYSKELAEGLAEVLKDLGRERAAVVHG-DGLDEASLLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  234 ATHIAELKDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALGRRKTEAGqkaAELIVMNAGPALYAADLATSL 313
Cdd:pfam00591 160 KTTVAELKDGEITEYTLTPEDFGLGRATLEALEGGSPKENADILKGVLGGKGSAAH---RDLVALNAGAALYLAGKADSL 236
                         250
                  ....*....|....*..
gi 489175677  314 HEGIQLAHDALHTGLAR 330
Cdd:pfam00591 237 KEGVAKALEVIDSGKAL 253
PLN02641 PLN02641
anthranilate phosphoribosyltransferase
1-334 2.71e-94

anthranilate phosphoribosyltransferase


Pssm-ID: 215345 [Multi-domain]  Cd Length: 343  Bit Score: 284.32  E-value: 2.71e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   1 MDIKGALNRIVNQLDLTTEEMQAVMRQIMTGQcTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELAdgVQLPTLKHVVDV 80
Cdd:PLN02641   2 ASFRQLIESLIQGTDLTEEEAEAALDFLLDDA-DEAQISAFLVLLRAKGETFEEIAGLARAMIKRA--RKVDGLVDAVDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  81 VGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKA 160
Cdd:PLN02641  79 VGTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVAIDLGPEGVKRCVEEVGIGFMMAPKYHPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 161 MKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRdGLDEFSLAAATHIAEL 240
Cdd:PLN02641 159 MKIVAPVRKKLKVKTVFNILGPMLNPARVPHAVVGVYHESLVEKMAKALQRFGMKRALVVHSE-GLDEMSPLGPGDVLEV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 241 KDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASLELIRDALgrrkteAGQKA--AELIVMNAGPALYAADLATSLHEGIQ 318
Cdd:PLN02641 238 TPEKIEEFSFDPLDFGIPRCTLEDLRGGDPDYNAKVLRDVL------SGEKGaiADALILNAAAALLVSGLAKTLAEGVA 311
                        330
                 ....*....|....*.
gi 489175677 319 LAHDALHTGLAREKMD 334
Cdd:PLN02641 312 LARETQESGKAIKTLD 327
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
4-338 5.57e-67

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 219.90  E-value: 5.57e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677   4 KGALNRIVNQL----DLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLKhVVD 79
Cdd:PRK09522 197 TNTLQPILEKLyqaqTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYL-FAD 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  80 VVGTGGDGANIFNVSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHK 159
Cdd:PRK09522 276 IVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHT 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 160 AMKYAAGPRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSrDGLDEFSLAAATHIAE 239
Cdd:PRK09522 356 GFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTIVAE 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 240 LKDGEVREYEVRPEDFGIKSQTLMGLEVDSPQASleliRDALGRRKTEAGQKAAELIVMNAGPALYAADLATSLHEGIQL 319
Cdd:PRK09522 435 LHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEEN----RDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQT 510
                        330
                 ....*....|....*....
gi 489175677 320 AHDALHTGLAREKMDELVA 338
Cdd:PRK09522 511 VLEVLRSGSAYDRVTALAA 529
Glycos_trans_3N pfam02885
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ...
4-66 7.13e-22

Glycosyl transferase family, helical bundle domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.


Pssm-ID: 460737 [Multi-domain]  Cd Length: 63  Bit Score: 87.43  E-value: 7.13e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489175677    4 KGALNRIVNQLDLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELA 66
Cdd:pfam02885   1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
PRK07394 PRK07394
hypothetical protein; Provisional
15-338 8.75e-17

hypothetical protein; Provisional


Pssm-ID: 168934 [Multi-domain]  Cd Length: 342  Bit Score: 79.96  E-value: 8.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  15 DLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLKHVVDVVGTGGDG----ANI 90
Cdd:PRK07394  21 DLTREEAADALKLMLLGEATPAQIGAFLIAHRIKRPTPEELAGMLDTYDELGPKLQSPSNQRPPIVFGMPYDGrsrtAPI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  91 FnvsSAASFVVAAAGGKVAKHGNRAVSGKSG--SADLLEAAGIYLE-LTSEQVARCIDTVGVGFMFAQVH----HKAMKY 163
Cdd:PRK07394 101 Y---PLTALILAAAGQPVVLHGGDRMPTKYGvpLVELWQGLGVDLTgLSLEQVQEGFEQTGLAFIYQPDHfplaESLIPY 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 164 aagpRRELGLRTLFNMLGPLTNP-AGVRHQVVGvF----TQELckpLAEVLKRLGSEHVLVVHSRDGLDEFSLAAATHIA 238
Cdd:PRK07394 178 ----RDEIGKRPPLATLELIWTPhQGDHHLVSG-FvhppTEAR---AWEALELRGETNFTTVKGLEGSCDLPISRTAIIG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 239 ELKDGEVREYEVRPEDFGIKSQTlmgLEVDSPQASLELIRDALGRRKTEAgQKAAeliVMNAGPALYAADLATSLHEGIQ 318
Cdd:PRK07394 250 RVQNGHFERLILHPRDYGCGGKD---VPWESTEEWLEQAQAALNGEPGPL-TQAL---IWNGGFYLWRAGISSSLEEGIE 322
                        330       340
                 ....*....|....*....|
gi 489175677 319 LAHDALHTGLAREKMDELVA 338
Cdd:PRK07394 323 KAEELLNSGKALQKLQQLIA 342
PRK09071 PRK09071
glycosyl transferase family protein;
16-250 1.30e-16

glycosyl transferase family protein;


Pssm-ID: 181637 [Multi-domain]  Cd Length: 323  Bit Score: 79.57  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  16 LTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMREladgvQLPTLKHVVDVvgtggD--------- 86
Cdd:PRK09071  21 LTREEARQAMGMILDGEVEDDQLGAFLMLLRVKEETAEELAGFVEAIRE-----RLQAPPLAVDL-----Dwpsyagkrr 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  87 -------GANIFnvssaasfvvAAAGGKVAKHGNRA-VSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFM----FA 154
Cdd:PRK09071  91 hlpwyllAAKLL----------AQNGYRVLLHGGGGhTAGRLYTEQLLEALGIPIARSWQEAEQALEEHNIAYLpledFA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677 155 QVHHKAMKYaagpRRELGLRTLFNMLGPLTNPAGVRHQVVGVFTQELCKPLAEVLKRLGSEHVLVVHSRDGLDEFSLAAA 234
Cdd:PRK09071 161 PQLQRMIDL----RNTLGLRSPINTLARLLNPLNAKASLQGIFHPGYQQLHREAARLLGDQNALVFKGEGGESERNPDVS 236
                        250
                 ....*....|....*.
gi 489175677 235 THIAELKDGEVREYEV 250
Cdd:PRK09071 237 TTLYGSRNGEAWDEEW 252
PRK08136 PRK08136
glycosyl transferase family protein; Provisional
15-190 1.57e-09

glycosyl transferase family protein; Provisional


Pssm-ID: 236160 [Multi-domain]  Cd Length: 317  Bit Score: 58.34  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  15 DLTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLKHVVdVVGTGGDGA-NIFNV 93
Cdd:PRK08136  19 DLDRDTARALYGAMLDGRVPDLELGAILIALRIKGESEAEMLGFLDAMQAHTIPLTPPAGRPMP-VVIPSYNGArKQANL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  94 SSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEAAGIYLELTSEQVARCIDTVGVGFMFAQVHHKAMKYAAGPRRELGL 173
Cdd:PRK08136  98 TPLLALLLAREGVPVLVHGVSEDPTRVTSAEIFEALGIPPTLHADQAQAKLAEGQPAFIPVGVLCPPLARLLALRWRMGV 177
                        170       180
                 ....*....|....*....|.
gi 489175677 174 R----TLFNMLGPLTNPAGVR 190
Cdd:PRK08136 178 RnsahTLAKLATPFAEGAALR 198
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
16-85 1.16e-03

Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439983 [Multi-domain]  Cd Length: 431  Bit Score: 40.41  E-value: 1.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489175677  16 LTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMRELADGVQLPTLK-HVVDVVGTGG 85
Cdd:COG0213   14 LTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSDIPgPKVDKHSTGG 84
deoA PRK05820
thymidine phosphorylase; Reviewed
16-155 1.52e-03

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 40.19  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175677  16 LTTEEMQAVMRQIMTGQCTDAQIGAFLMGMRMKSETIDEIVGAVAVMR---ELADGVQLPTLKHVVDVVGTGGDGANIfn 92
Cdd:PRK05820  17 LSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRdsgEVLDWSSLNLNGPIVDKHSTGGVGDKI-- 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489175677  93 vSSAASFVVAAAGGKVAKHGNRAVSGKSGSADLLEA-AGIYLELTSEQVARCIDTVGVgFMFAQ 155
Cdd:PRK05820  95 -SLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAiPGYRAFPSNDRFREILKDVGV-AIIGQ 156
 
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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