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Protein

Anthranilate phosphoribosyltransferase

Gene

trpD

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation4 PublicationsNote: Binds 2 magnesium ions per monomer.UniRule annotation4 Publications

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Phosphoribosyl isomerase A (priA), Phosphoribosyl isomerase A (priA)
  4. Indole-3-glycerol phosphate synthase (trpC), Indole-3-glycerol phosphate synthase (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107Anthranilate 1; via carbonyl oxygenUniRule annotation1
Binding sitei107Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation4 Publications1
Binding sitei115PhosphoribosylpyrophosphateUniRule annotation4 Publications1
Metal bindingi119Magnesium 11
Binding sitei138Anthranilate 11
Binding sitei147Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation4 Publications1
Binding sitei193Anthranilate 21
Metal bindingi251Magnesium 21
Metal bindingi252Magnesium 11
Metal bindingi252Magnesium 21

GO - Molecular functioni

GO - Biological processi

  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • growth Source: MTBBASE
  • tryptophan biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6402-MONOMER.
UniPathwayiUPA00035; UER00041.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.18UniRule annotation)
Gene namesi
Name:trpDUniRule annotation
Ordered Locus Names:Rv2192c
ORF Names:MTCY190.03c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2192c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001544612 – 370Anthranilate phosphoribosyltransferaseAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP9WFX5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation4 Publications

Protein-protein interaction databases

STRINGi83332.Rv2192c.

Structurei

Secondary structure

1370
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 35Combined sources9
Helixi44 – 53Combined sources10
Helixi59 – 72Combined sources14
Helixi76 – 89Combined sources14
Beta strandi103 – 107Combined sources5
Beta strandi111 – 113Combined sources3
Helixi118 – 128Combined sources11
Beta strandi133 – 137Combined sources5
Beta strandi141 – 145Combined sources5
Helixi147 – 153Combined sources7
Helixi162 – 172Combined sources11
Beta strandi173 – 178Combined sources6
Helixi179 – 182Combined sources4
Helixi184 – 189Combined sources6
Helixi190 – 196Combined sources7
Helixi201 – 204Combined sources4
Helixi206 – 208Combined sources3
Beta strandi215 – 220Combined sources6
Helixi224 – 226Combined sources3
Helixi227 – 236Combined sources10
Beta strandi240 – 246Combined sources7
Turni247 – 249Combined sources3
Beta strandi250 – 252Combined sources3
Beta strandi255 – 257Combined sources3
Beta strandi259 – 265Combined sources7
Beta strandi268 – 274Combined sources7
Helixi276 – 279Combined sources4
Helixi286 – 289Combined sources4
Helixi294 – 305Combined sources12
Helixi311 – 328Combined sources18
Turni329 – 331Combined sources3
Helixi336 – 352Combined sources17
Helixi355 – 368Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZVWX-ray2.30A/B1-370[»]
2BPQX-ray1.90A/B2-370[»]
3QQSX-ray1.97A/B/C/D2-370[»]
3QR9X-ray1.87A/B2-370[»]
3QS8X-ray2.00A/B/C/D2-370[»]
3QSAX-ray2.18A/B2-370[»]
3R6CX-ray1.83A/B2-370[»]
3R88X-ray1.73A/B2-370[»]
3TWPX-ray1.83A/B/C/D2-370[»]
3UU1X-ray1.82A/B/C/D2-370[»]
4GIUX-ray1.67A/B1-370[»]
4GKMX-ray1.67A/B2-370[»]
4IJ1X-ray1.79A/B2-370[»]
4M0RX-ray1.96A/B2-370[»]
4N5VX-ray1.90A/B1-370[»]
4N8QX-ray2.08A/B1-370[»]
4N93X-ray2.03A/B1-370[»]
4OWMX-ray1.99A/B1-370[»]
4OWNX-ray2.11A/B1-370[»]
4OWOX-ray1.99A/B1-370[»]
4OWQX-ray1.89A/B1-370[»]
4OWSX-ray2.43A/B1-370[»]
4OWUX-ray1.89A/B1-370[»]
4OWVX-ray1.90A/B1-370[»]
4X58X-ray1.75A/B1-370[»]
4X59X-ray1.80A/B1-370[»]
4X5AX-ray1.93A/B1-370[»]
4X5BX-ray2.47A/B1-370[»]
4X5CX-ray2.33A/B1-370[»]
4X5DX-ray2.30A/B1-370[»]
4X5EX-ray1.77A/B1-370[»]
5BNEX-ray2.15A/B/C/D2-370[»]
5BYTX-ray2.00A/B2-370[»]
5C1RX-ray1.80A/B2-370[»]
5C2LX-ray2.01A/B2-370[»]
5C7SX-ray2.10A/B2-370[»]
ProteinModelPortaliP9WFX5.
SMRiP9WFX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 111Phosphoribosylpyrophosphate binding2
Regioni117 – 120Phosphoribosylpyrophosphate binding4
Regioni135 – 143Phosphoribosylpyrophosphate binding9

Sequence similaritiesi

Belongs to the anthranilate phosphoribosyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108I0Q. Bacteria.
COG0547. LUCA.
KOiK00766.
OMAiWLVHGSD.
PhylomeDBiP9WFX5.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
HAMAPiMF_00211. TrpD. 1 hit.
InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
[Graphical view]
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
TIGRFAMsiTIGR01245. trpD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WFX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSAEGSSG GSRGGSPKAE AASVPSWPQI LGRLTDNRDL ARGQAAWAMD
60 70 80 90 100
QIMTGNARPA QIAAFAVAMT MKAPTADEVG ELAGVMLSHA HPLPADTVPD
110 120 130 140 150
DAVDVVGTGG DGVNTVNLST MAAIVVAAAG VPVVKHGNRA ASSLSGGADT
160 170 180 190 200
LEALGVRIDL GPDLVARSLA EVGIGFCFAP RFHPSYRHAA AVRREIGVPT
210 220 230 240 250
VFNLLGPLTN PARPRAGLIG CAFADLAEVM AGVFAARRSS VLVVHGDDGL
260 270 280 290 300
DELTTTTTST IWRVAAGSVD KLTFDPAGFG FARAQLDQLA GGDAQANAAA
310 320 330 340 350
VRAVLGGARG PVRDAVVLNA AGAIVAHAGL SSRAEWLPAW EEGLRRASAA
360 370
IDTGAAEQLL ARWVRFGRQI
Length:370
Mass (Da):37,740
Last modified:April 16, 2014 - v1
Checksum:i23C8B67D6C33E18D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44969.1.
PIRiA70784.
RefSeqiNP_216708.1. NC_000962.3.
WP_003411387.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP44969; CCP44969; Rv2192c.
GeneIDi887681.
KEGGimtu:Rv2192c.
mtv:RVBD_2192c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44969.1.
PIRiA70784.
RefSeqiNP_216708.1. NC_000962.3.
WP_003411387.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZVWX-ray2.30A/B1-370[»]
2BPQX-ray1.90A/B2-370[»]
3QQSX-ray1.97A/B/C/D2-370[»]
3QR9X-ray1.87A/B2-370[»]
3QS8X-ray2.00A/B/C/D2-370[»]
3QSAX-ray2.18A/B2-370[»]
3R6CX-ray1.83A/B2-370[»]
3R88X-ray1.73A/B2-370[»]
3TWPX-ray1.83A/B/C/D2-370[»]
3UU1X-ray1.82A/B/C/D2-370[»]
4GIUX-ray1.67A/B1-370[»]
4GKMX-ray1.67A/B2-370[»]
4IJ1X-ray1.79A/B2-370[»]
4M0RX-ray1.96A/B2-370[»]
4N5VX-ray1.90A/B1-370[»]
4N8QX-ray2.08A/B1-370[»]
4N93X-ray2.03A/B1-370[»]
4OWMX-ray1.99A/B1-370[»]
4OWNX-ray2.11A/B1-370[»]
4OWOX-ray1.99A/B1-370[»]
4OWQX-ray1.89A/B1-370[»]
4OWSX-ray2.43A/B1-370[»]
4OWUX-ray1.89A/B1-370[»]
4OWVX-ray1.90A/B1-370[»]
4X58X-ray1.75A/B1-370[»]
4X59X-ray1.80A/B1-370[»]
4X5AX-ray1.93A/B1-370[»]
4X5BX-ray2.47A/B1-370[»]
4X5CX-ray2.33A/B1-370[»]
4X5DX-ray2.30A/B1-370[»]
4X5EX-ray1.77A/B1-370[»]
5BNEX-ray2.15A/B/C/D2-370[»]
5BYTX-ray2.00A/B2-370[»]
5C1RX-ray1.80A/B2-370[»]
5C2LX-ray2.01A/B2-370[»]
5C7SX-ray2.10A/B2-370[»]
ProteinModelPortaliP9WFX5.
SMRiP9WFX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2192c.

Proteomic databases

PaxDbiP9WFX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44969; CCP44969; Rv2192c.
GeneIDi887681.
KEGGimtu:Rv2192c.
mtv:RVBD_2192c.

Organism-specific databases

TubercuListiRv2192c.

Phylogenomic databases

eggNOGiENOG4108I0Q. Bacteria.
COG0547. LUCA.
KOiK00766.
OMAiWLVHGSD.
PhylomeDBiP9WFX5.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00041.
BioCyciMTBH37RV:G185E-6402-MONOMER.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
HAMAPiMF_00211. TrpD. 1 hit.
InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
[Graphical view]
PfamiPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
TIGRFAMsiTIGR01245. trpD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTRPD_MYCTU
AccessioniPrimary (citable) accession number: P9WFX5
Secondary accession number(s): L0T8W2, P66992, Q10382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.