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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Anthranilate 1; via carbonyl oxygenUniRule annotation
Binding sitei107 – 1071Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation4 Publications
Binding sitei115 – 1151PhosphoribosylpyrophosphateUniRule annotation4 Publications
Metal bindingi119 – 1191Magnesium 1
Binding sitei138 – 1381Anthranilate 1
Binding sitei147 – 1471Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation4 Publications
Binding sitei193 – 1931Anthranilate 2
Metal bindingi251 – 2511Magnesium 2
Metal bindingi252 – 2521Magnesium 1
Metal bindingi252 – 2521Magnesium 2

GO - Molecular functioni

GO - Biological processi

  • 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

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 370369Anthranilate phosphoribosyltransferasePRO_0000154461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP9WFX5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation4 Publications

Protein-protein interaction databases

STRINGi83332.Rv2192c.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 359Combined sources
Helixi44 – 5310Combined sources
Helixi59 – 7214Combined sources
Helixi76 – 8914Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi111 – 1133Combined sources
Helixi118 – 12811Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi141 – 1455Combined sources
Helixi147 – 1537Combined sources
Helixi162 – 17211Combined sources
Beta strandi173 – 1786Combined sources
Helixi179 – 1824Combined sources
Helixi184 – 1896Combined sources
Helixi190 – 1967Combined sources
Helixi201 – 2044Combined sources
Helixi206 – 2083Combined sources
Beta strandi215 – 2206Combined sources
Helixi224 – 2263Combined sources
Helixi227 – 23610Combined sources
Beta strandi240 – 2467Combined sources
Turni247 – 2493Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi268 – 2747Combined sources
Helixi276 – 2794Combined sources
Helixi286 – 2894Combined sources
Helixi294 – 30512Combined sources
Helixi311 – 32818Combined sources
Turni329 – 3313Combined sources
Helixi336 – 35217Combined sources
Helixi355 – 36814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5C2LX-ray2.01A/B2-370[»]
ProteinModelPortaliP9WFX5.
SMRiP9WFX5. Positions 25-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 1112Phosphoribosylpyrophosphate binding
Regioni117 – 1204Phosphoribosylpyrophosphate binding
Regioni135 – 1439Phosphoribosylpyrophosphate binding

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
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[»]
5C2LX-ray2.01A/B2-370[»]
ProteinModelPortaliP9WFX5.
SMRiP9WFX5. Positions 25-370.
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.

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: September 7, 2016
This is version 23 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.