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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Pathway: 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. Putative anthranilate synthase component II (HI_1171), Anthranilate synthase component 2 (trpG), Anthranilate synthase component 1 (trpE)
  2. Anthranilate phosphoribosyltransferase (trpD)
  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

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:HI_1389.1
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Tryptophan biosynthesis protein TrpCFPRO_0000154279Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi71421.HI1389.1.

Structurei

3D structure databases

ProteinModelPortaliP46451.
SMRiP46451. Positions 16-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 275263Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni276 – 477202N-(5'-phosphoribosyl)anthranilate isomeraseAdd
BLAST

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

eggNOGiCOG0134.
KOiK13498.
OMAiSFILECK.
OrthoDBiEOG6WT8JX.
PhylomeDBiP46451.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
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.

P46451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMITQDFTKP IDSATVLQKI VLDKAQWVKA KEKEFPLSQF KQNIQNSDRS
60 70 80 90 100
FYDALAKGTH QKPAYILECK KASPSKGLIR AEFNLEEIAN VYKHYASAVS
110 120 130 140 150
VLTDEKYFQG NFEFLPLVRD IVSQPVLCKD FMISEYQVYL ARYYQVDAIL
160 170 180 190 200
LMLSVVNDET YRVLADLAHS LGMGVLTETS NEEEFERALA LGAKIIGVNN
210 220 230 240 250
RNLHDLTVDL NRVVELTKKY ADCIPADVRI ISESGIYNHK QIHQLQKVAH
260 270 280 290 300
GFLIGSSLMG NQDLNNAVRS VIFGENKVCG LTRAQDVKIV YENGALYGGL
310 320 330 340 350
IFAEHSKRSV SLRQAQELVT AAPLRFVGVF QNQEIDFIVK IASQLQLYAV
360 370 380 390 400
QLHGAETEAF ITALRQQLPK NTQIWKAISV NTEAQSAVDF TDDLNVDRYI
410 420 430 440 450
FDSQTANQQG GTGKTFDWSL IPENLKHKII LAGGISPNNV EQAIAQGCLG
460 470
LDLNSGVESS AGVKDQEKVR LVFNNIY
Length:477
Mass (Da):53,306
Last modified:November 1, 1995 - v1
Checksum:iB1435FAEFA24379E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC23036.1.
RefSeqiNP_439543.1. NC_000907.1.
WP_005693972.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23036; AAC23036; HI_1389.1.
GeneIDi950301.
KEGGihin:HI1389.1.
PATRICi20191475. VBIHaeInf48452_1448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC23036.1.
RefSeqiNP_439543.1. NC_000907.1.
WP_005693972.1. NC_000907.1.

3D structure databases

ProteinModelPortaliP46451.
SMRiP46451. Positions 16-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1389.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC23036; AAC23036; HI_1389.1.
GeneIDi950301.
KEGGihin:HI1389.1.
PATRICi20191475. VBIHaeInf48452_1448.

Phylogenomic databases

eggNOGiCOG0134.
KOiK13498.
OMAiSFILECK.
OrthoDBiEOG6WT8JX.
PhylomeDBiP46451.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Koonin E.V., Rudd K.E.
    Submitted (SEP-1995) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiTRPC_HAEIN
AccessioniPrimary (citable) accession number: P46451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 27, 2015
This is version 106 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. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.