Skip Header

Contribute Send feedback
Read comments (?) or add your own

P46451 (TRPC_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

  1. Indole-3-glycerol phosphate synthase
    Short name=IGPS
    EC=4.1.1.48
  2. N-(5'-phospho-ribosyl)anthranilate isomerase
    Short name=PRAI
    EC=5.3.1.24
Gene names
Name:trpC
Ordered Locus Names:HI_1389.1
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00134_B

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.

Subunit structure

Monomer By similarity.

Sequence similarities

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154279

Regions

Region13 – 275263Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region276 – 477202N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
P46451 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B1435FAEFA24379E

FASTA47753,306
        10         20         30         40         50         60 
MMITQDFTKP IDSATVLQKI VLDKAQWVKA KEKEFPLSQF KQNIQNSDRS FYDALAKGTH 

        70         80         90        100        110        120 
QKPAYILECK KASPSKGLIR AEFNLEEIAN VYKHYASAVS VLTDEKYFQG NFEFLPLVRD 

       130        140        150        160        170        180 
IVSQPVLCKD FMISEYQVYL ARYYQVDAIL LMLSVVNDET YRVLADLAHS LGMGVLTETS 

       190        200        210        220        230        240 
NEEEFERALA LGAKIIGVNN RNLHDLTVDL NRVVELTKKY ADCIPADVRI ISESGIYNHK 

       250        260        270        280        290        300 
QIHQLQKVAH GFLIGSSLMG NQDLNNAVRS VIFGENKVCG LTRAQDVKIV YENGALYGGL 

       310        320        330        340        350        360 
IFAEHSKRSV SLRQAQELVT AAPLRFVGVF QNQEIDFIVK IASQLQLYAV QLHGAETEAF 

       370        380        390        400        410        420 
ITALRQQLPK NTQIWKAISV NTEAQSAVDF TDDLNVDRYI FDSQTANQQG GTGKTFDWSL 

       430        440        450        460        470 
IPENLKHKII LAGGISPNNV EQAIAQGCLG LDLNSGVESS AGVKDQEKVR LVFNNIY

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC23036.1.
RefSeqNP_439543.1. NC_000907.1.

3D structure databases

ProteinModelPortalP46451.
SMRP46451. Positions 16-278.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI1389.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC23036; AAC23036; HI_1389.1.
GeneID950301.
KEGGhin:HI1389.1.
PATRIC20191475. VBIHaeInf48452_1448.

Phylogenomic databases

eggNOGCOG0134.
KOK13498.
OMAYILECKK.
ProtClustDBPRK09427.

Enzyme and pathway databases

UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00134_B. IGPS_B. Fused.
MF_00135. PRAI. Fused.
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. RibP_bind_barrel. 2 hits.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_HAEIN
AccessionPrimary (citable) accession number: P46451
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents