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P22098 (TRPC_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Synonyms:trpC-TRPF
Ordered Locus Names:VP1959
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length481 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.

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 – 481481Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154286

Regions

Region1 – 283283Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region284 – 481198N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Experimental info

Sequence conflict2031R → K in CAA35034. Ref.1
Sequence conflict4491G → A in CAA35034. Ref.1
Sequence conflict4761H → R in CAA35034. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22098 [UniParc].

Last modified April 4, 2003. Version 2.
Checksum: BC575AD8FB57FC00

FASTA48152,974
        10         20         30         40         50         60 
MKMTDFNTQQ ANNLSEHVSK KEAEMAEVLA KIVRDKYQWV AERKASQHLS TFQSDLLPSD 

        70         80         90        100        110        120 
RSFYDALSGD KTVFITECKK ASPSKGLIRN DFDLDYIASV YNNYADAISV LTDEKYFQGS 

       130        140        150        160        170        180 
FDFLPQVRRQ VKQPVLCKDF MVDTYQVYLA RHYGADAVLL MLSVLNDEEY KALEEAAHSL 

       190        200        210        220        230        240 
NMGILTEVSN EEELHRAVQL GARVIGINNR NLRDLTTDLN RTKALAPTIR KLAPNATVIS 

       250        260        270        280        290        300 
ESGIYTHQQV RDLAEYADGF LIGSSLMAED NLELAVRKVT LGENKVCGLT HPDDAAKAYQ 

       310        320        330        340        350        360 
AGAVFGGLIF VEKSKRAVDF ESARLTMSGA PLNYVGVFQN HDVDYVASIV TSLGLKAVQL 

       370        380        390        400        410        420 
HGLEDQEYVN QLKTELPVGV EIWKAYGVAD TKPSLLADNI DRHLLDAQVG TQTGGTGHVF 

       430        440        450        460        470        480 
DWSLIGDPSQ IMLAGGLSPE NAQQAAKLGC LGLDLNSGVE SAPGKKDSQK LQAAFHAIRN 


Y 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and features of the tryptophan operon of Vibrio parahemolyticus."
Crawford I.P., Han C.Y., Silverman M.
DNA Seq. 1:189-196(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BB22.
[2]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17149 Genomic DNA. Translation: CAA35034.1.
BA000031 Genomic DNA. Translation: BAC60222.1.
RefSeqNP_798338.1. NC_004603.1.

3D structure databases

ProteinModelPortalP22098.
SMRP22098. Positions 25-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP1959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60222; BAC60222; BAC60222.
GeneID1189470.
KEGGvpa:VP1959.
PATRIC20142086. VBIVibPar50997_1874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280458.
KOK13498.
OMAEKYFQGD.
OrthoDBEOG6WT8JX.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2014-MONOMER.
UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 2 hits.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_VIBPA
AccessionPrimary (citable) accession number: P22098
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 4, 2003
Last modified: May 14, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways