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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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. Anthranilate synthase component 1 (trpE)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. 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.

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase

Keywords - Biological processi

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

Enzyme and pathway databases

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
Ordered Locus Names:PM0580
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
Proteomesi
  • UP000000809 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001542821 – 469Tryptophan biosynthesis protein TrpCFAdd BLAST469

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi272843.PM0580.

Structurei

3D structure databases

ProteinModelPortaliP57855.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 267Indole-3-glycerol phosphate synthaseAdd BLAST267
Regioni268 – 469N-(5'-phosphoribosyl)anthranilate isomeraseAdd BLAST202

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.
KOiK13498.
OMAiTSFILEC.

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.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P57855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQAFPSILQ KIIQDKTTWI AEKQAQLPLA SFQDQLERSD RDFYQAMQQG
60 70 80 90 100
SKQRPSYILE CKKASPSKGL IRAAFDLTEI AEVYQHYATV ISVLTDEKYF
110 120 130 140 150
QGHFADIAQV RQRVTQPILC KDFILSEYQV YLARYAQADA ILLMLSVLND
160 170 180 190 200
ERYTQLATLA HQLGMGVLTE TSNEAEFARA LALKAKVIGV NNRNLHDLSV
210 220 230 240 250
DIQRVAQITQ HYADQIPPET KIISESGIYQ HQQIRDLRHV ADGFLIGSSL
260 270 280 290 300
MQHTDLNHAV RSLLFGEHKV CGLTRPQDVR AVYQQGALYG GLIFVTHSKR
310 320 330 340 350
CISLRQAQEL VTQAPLRFVG VFQDQSIAFI CHLATQLRLH AVQLHGNESH
360 370 380 390 400
EFIRQLRDEL PVNCEIWRAI CIESSGTSPC QIVENKNIDR YIFDSKTHQQ
410 420 430 440 450
RGGTGKTFDW QLIPHHLKPK SMLAGGITPE NIPLALAQGC LGLDLNSGLE
460
TYPGVKSHQK VVAAFAQLR
Length:469
Mass (Da):52,851
Last modified:April 27, 2001 - v1
Checksum:iCD1FD2866ADF10C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02664.1.
RefSeqiWP_010906737.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02664; AAK02664; PM0580.
GeneIDi1243927.
KEGGipmu:PM0580.
PATRICi22870342. VBIPasMul88067_0587.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02664.1.
RefSeqiWP_010906737.1. NC_002663.1.

3D structure databases

ProteinModelPortaliP57855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272843.PM0580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK02664; AAK02664; PM0580.
GeneIDi1243927.
KEGGipmu:PM0580.
PATRICi22870342. VBIPasMul88067_0587.

Phylogenomic databases

eggNOGiENOG4105DK0. Bacteria.
COG0134. LUCA.
COG0135. LUCA.
HOGENOMiHOG000280458.
KOiK13498.
OMAiTSFILEC.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

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.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPC_PASMU
AccessioniPrimary (citable) accession number: P57855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: November 2, 2016
This is version 99 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.