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Protein

Indole-3-glycerol phosphate synthase

Gene

trpC

Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathway: L-tryptophan biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
  4. Indole-3-glycerol phosphate synthase (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

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciPMAR74546:GHRG-1425-MONOMER.
UniPathwayiUPA00035; UER00043.

Names & Taxonomyi

Protein namesi
Recommended name:
Indole-3-glycerol phosphate synthaseUniRule annotation (EC:4.1.1.48UniRule annotation)
Short name:
IGPSUniRule annotation
Gene namesi
Name:trpCUniRule annotation
Ordered Locus Names:PMT9312_1393
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Indole-3-glycerol phosphate synthasePRO_1000018523Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi74546.PMT9312_1393.

Structurei

3D structure databases

ProteinModelPortaliQ319J2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpC family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0134.
HOGENOMiHOG000230463.
KOiK01609.
OMAiDIAQSYA.
OrthoDBiEOG6WT8JX.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00134_B. IGPS_B.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q319J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIRRRPPNP TVRVENLEYA VPHREAQAKN ILEEIVWHKD IEIKNFKKIV
60 70 80 90 100
SLEDLIKKIE NLPDPKDFYK NILESKIKPG LIAEIKKASP SKGVIRKDFN
110 120 130 140 150
PEDIAICYEE LGASCISVLT DKRFFQGSYE ILETVRKSTN LPLLCKDFII
160 170 180 190 200
SAYQIYKARV SGADAILLIA AILSDDDLIY LKKIADNLKM SVLVEVHNDN
210 220 230 240 250
ELERILKLKS FNLIGINNRD LKTFKTDLKT SIELMHIYAD IFLKQNILPI
260 270 280 290
SESGINCAQD LESLRSIGIK GVLIGETFMR ESDIEKSFKK LFNSI
Length:295
Mass (Da):33,738
Last modified:December 6, 2005 - v1
Checksum:i7CD896FA9001EB19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB50453.1.
RefSeqiWP_011376939.1. NC_007577.1.
YP_397889.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB50453; ABB50453; PMT9312_1393.
KEGGipmi:PMT9312_1393.
PATRICi23006718. VBIProMar70153_1526.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB50453.1.
RefSeqiWP_011376939.1. NC_007577.1.
YP_397889.1. NC_007577.1.

3D structure databases

ProteinModelPortaliQ319J2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74546.PMT9312_1393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB50453; ABB50453; PMT9312_1393.
KEGGipmi:PMT9312_1393.
PATRICi23006718. VBIProMar70153_1526.

Phylogenomic databases

eggNOGiCOG0134.
HOGENOMiHOG000230463.
KOiK01609.
OMAiDIAQSYA.
OrthoDBiEOG6WT8JX.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00043.
BioCyciPMAR74546:GHRG-1425-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00134_B. IGPS_B.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiTRPC_PROM9
AccessioniPrimary (citable) accession number: Q319J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 27, 2015
This is version 66 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

Documents

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