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P57855 (TRPC_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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
Ordered Locus Names:PM0580
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length469 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 – 469469Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154282

Regions

Region1 – 267267Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region268 – 469202N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
P57855 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: CD1FD2866ADF10C8

FASTA46952,851
        10         20         30         40         50         60 
MTQAFPSILQ KIIQDKTTWI AEKQAQLPLA SFQDQLERSD RDFYQAMQQG SKQRPSYILE 

        70         80         90        100        110        120 
CKKASPSKGL IRAAFDLTEI AEVYQHYATV ISVLTDEKYF QGHFADIAQV RQRVTQPILC 

       130        140        150        160        170        180 
KDFILSEYQV YLARYAQADA ILLMLSVLND ERYTQLATLA HQLGMGVLTE TSNEAEFARA 

       190        200        210        220        230        240 
LALKAKVIGV NNRNLHDLSV DIQRVAQITQ HYADQIPPET KIISESGIYQ HQQIRDLRHV 

       250        260        270        280        290        300 
ADGFLIGSSL MQHTDLNHAV RSLLFGEHKV CGLTRPQDVR AVYQQGALYG GLIFVTHSKR 

       310        320        330        340        350        360 
CISLRQAQEL VTQAPLRFVG VFQDQSIAFI CHLATQLRLH AVQLHGNESH EFIRQLRDEL 

       370        380        390        400        410        420 
PVNCEIWRAI CIESSGTSPC QIVENKNIDR YIFDSKTHQQ RGGTGKTFDW QLIPHHLKPK 

       430        440        450        460 
SMLAGGITPE NIPLALAQGC LGLDLNSGLE TYPGVKSHQK VVAAFAQLR 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK02664.1.
RefSeqNP_245517.1. NC_002663.1.

3D structure databases

ProteinModelPortalP57855.
SMRP57855. Positions 5-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02664; AAK02664; PM0580.
GeneID1243927.
KEGGpmu:PM0580.
PATRIC22870342. VBIPasMul88067_0587.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280458.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-601-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_PASMU
AccessionPrimary (citable) accession number: P57855
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: February 19, 2014
This is version 82 of the entry and version 1 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