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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain.

Catalytic activityi

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 3 and 4 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
  2. Bifunctional protein TrpGD (trpGD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
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.

GO - Molecular functioni

  • indole-3-glycerol-phosphate synthase activity Source: EcoCyc
  • phosphoribosylanthranilate isomerase activity Source: EcoCyc

GO - Biological processi

  • tryptophan biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionDecarboxylase, Isomerase, Lyase, Multifunctional enzyme
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:PRAI-IGPS
MetaCyc:PRAI-IGPS
BRENDAi5.3.1.24 2026
UniPathwayiUPA00035; UER00042
UPA00035; UER00043

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan biosynthesis protein TrpCF
Including the following 2 domains:
Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
Short name:
IGPS
N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
Short name:
PRAI
Gene namesi
Name:trpC
Synonyms:trpF
Ordered Locus Names:b1262, JW1254
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11026 trpC

Pathology & Biotechi

Chemistry databases

DrugBankiDB03543 1-(O-Carboxy-Phenylamino)-1-Deoxy-D-Ribulose-5-Phosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001542771 – 453Tryptophan biosynthesis protein TrpCFAdd BLAST453

Proteomic databases

EPDiP00909
PaxDbiP00909
PRIDEiP00909

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4260122, 4 interactors
IntActiP00909, 7 interactors
STRINGi316385.ECDH10B_1377

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 23Combined sources19
Helixi26 – 28Combined sources3
Helixi30 – 32Combined sources3
Helixi40 – 44Combined sources5
Beta strandi46 – 48Combined sources3
Beta strandi50 – 55Combined sources6
Beta strandi57 – 59Combined sources3
Turni60 – 62Combined sources3
Beta strandi63 – 65Combined sources3
Helixi71 – 78Combined sources8
Turni79 – 81Combined sources3
Beta strandi83 – 88Combined sources6
Turni92 – 94Combined sources3
Helixi100 – 107Combined sources8
Beta strandi112 – 116Combined sources5
Helixi121 – 129Combined sources9
Beta strandi133 – 138Combined sources6
Turni139 – 141Combined sources3
Helixi144 – 156Combined sources13
Beta strandi160 – 165Combined sources6
Helixi168 – 176Combined sources9
Beta strandi180 – 187Combined sources8
Turni189 – 191Combined sources3
Helixi197 – 206Combined sources10
Beta strandi210 – 216Combined sources7
Helixi221 – 227Combined sources7
Turni228 – 230Combined sources3
Beta strandi232 – 236Combined sources5
Helixi238 – 241Combined sources4
Helixi246 – 255Combined sources10
Helixi266 – 275Combined sources10
Beta strandi278 – 283Combined sources6
Helixi294 – 303Combined sources10
Beta strandi307 – 314Combined sources8
Helixi317 – 327Combined sources11
Beta strandi330 – 334Combined sources5
Helixi336 – 338Combined sources3
Helixi340 – 349Combined sources10
Beta strandi354 – 361Combined sources8
Beta strandi363 – 365Combined sources3
Beta strandi376 – 381Combined sources6
Helixi392 – 395Combined sources4
Beta strandi403 – 408Combined sources6
Turni411 – 413Combined sources3
Helixi414 – 418Combined sources5
Beta strandi423 – 427Combined sources5
Helixi429 – 431Combined sources3
Beta strandi432 – 434Combined sources3
Helixi440 – 451Combined sources12

3D structure databases

ProteinModelPortaliP00909
SMRiP00909
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00909

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 257Indole-3-glycerol phosphate synthaseAdd BLAST257
Regioni258 – 453N-(5'-phosphoribosyl)anthranilate isomeraseAdd BLAST196

Sequence similaritiesi

In the N-terminal section; belongs to the TrpC family.Curated
In the C-terminal section; belongs to the TrpF family.Curated

Phylogenomic databases

eggNOGiENOG4105DK0 Bacteria
COG0134 LUCA
COG0135 LUCA
HOGENOMiHOG000280458
InParanoidiP00909
KOiK13498

Family and domain databases

CDDicd00331 IGPS, 1 hit
cd00405 PRAI, 1 hit
Gene3Di3.20.20.70, 2 hits
HAMAPiMF_00134_B IGPS_B, 1 hit
MF_00135 PRAI, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR013798 Indole-3-glycerol_P_synth
IPR001468 Indole-3-GlycerolPSynthase_CS
IPR001240 PRAI
IPR011060 RibuloseP-bd_barrel
PfamiView protein in Pfam
PF00218 IGPS, 1 hit
PF00697 PRAI, 1 hit
SUPFAMiSSF51366 SSF51366, 2 hits
PROSITEiView protein in PROSITE
PS00614 IGPS, 1 hit

Sequencei

Sequence statusi: Complete.

P00909-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA
60 70 80 90 100
FILECKKASP SKGVIRDDFD PARIAAIYKH YASAISVLTD EKYFQGSFNF
110 120 130 140 150
LPIVSQIAPQ PILCKDFIID PYQIYLARYY QADACLLMLS VLDDDQYRQL
160 170 180 190 200
AAVAHSLEMG VLTEVSNEEE QERAIALGAK VVGINNRDLR DLSIDLNRTR
210 220 230 240 250
ELAPKLGHNV TVISESGINT YAQVRELSHF ANGFLIGSAL MAHDDLHAAV
260 270 280 290 300
RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV
310 320 330 340 350
MAAAPLQYVG VFRNHDIADV VDKAKVLSLA AVQLHGNEEQ LYIDTLREAL
360 370 380 390 400
PAHVAIWKAL SVGETLPARE FQHVDKYVLD NGQGGSGQRF DWSLLNGQSL
410 420 430 440 450
GNVLLAGGLG ADNCVEAAQT GCAGLDFNSA VESQPGIKDA RLLASVFQTL

RAY
Length:453
Mass (Da):49,492
Last modified:March 19, 2014 - v4
Checksum:i09D5DA2353291F33
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31Missing in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti95Q → R in CAA23664 (PubMed:7007653).Curated1
Sequence conflicti95Q → R in AAA57299 (PubMed:7007653).Curated1
Sequence conflicti95Q → R in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti285Missing in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti294V → D in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti330A → V in CAA23664 (PubMed:7007653).Curated1
Sequence conflicti330A → V in AAA57299 (PubMed:7007653).Curated1
Sequence conflicti330A → V in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti399S → T in CAA23664 (PubMed:7007653).Curated1
Sequence conflicti399S → T in AAA57299 (PubMed:7007653).Curated1
Sequence conflicti399S → T in CAA23673 (PubMed:7038627).Curated1
Sequence conflicti399S → T in AAB60033 (PubMed:8095913).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00366 Genomic DNA Translation: CAA23664.1
V00372 Genomic DNA Translation: CAA23673.1
J01714 Genomic DNA Translation: AAA57299.1
U23489 Genomic DNA Translation: AAB60033.1
U00096 Genomic DNA Translation: AAC74344.3
AP009048 Genomic DNA Translation: BAA14794.1
PIRiA64874 GWEC
RefSeqiNP_415778.3, NC_000913.3
WP_000983871.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74344; AAC74344; b1262
BAA14794; BAA14794; BAA14794
GeneIDi945519
KEGGiecj:JW1254
eco:b1262
PATRICifig|511145.12.peg.1312

Similar proteinsi

Entry informationi

Entry nameiTRPC_ECOLI
AccessioniPrimary (citable) accession number: P00909
Secondary accession number(s): P78059, P78234, P94704
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 19, 2014
Last modified: January 31, 2018
This is version 163 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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

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