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Q8X7B7

- TRPC_ECO57

UniProt

Q8X7B7 - TRPC_ECO57

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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Escherichia coli O157:H7
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. indole-3-glycerol-phosphate synthase activity Source: UniProtKB-EC
  2. phosphoribosylanthranilate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. tryptophan biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciECOL386585:GJFA-1810-MONOMER.
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:Z2549, ECs1834
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Tryptophan biosynthesis protein TrpCFPRO_0000154278Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi155864.Z2549.

Structurei

3D structure databases

ProteinModelPortaliQ8X7B7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 257257Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni258 – 453196N-(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.
HOGENOMiHOG000280458.
KOiK13498.
OMAiEKYFQGD.
OrthoDBiEOG6WT8JX.

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_dom.
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.

Q8X7B7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA
60 70 80 90 100
FILECKKASP SKGVICDDFD PARIAAIYKH YASAISVLTD EKYFQGSFDF
110 120 130 140 150
LPIVSQIAPQ PILCKDFIID PYQIYLARYY QADACLLMLS VLDDEQYRQL
160 170 180 190 200
AAVAHSLKMG VLTEVSNEEE LERAIALGAK VVGINNRDLR DLSIDLNRTR
210 220 230 240 250
ELAPKLGHNV TVISESGINT YAQVRELSHF ADGFLIGSAL MAHDDLHAAV
260 270 280 290 300
RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV
310 320 330 340 350
MAAAPLQYVG VFRNHDIADV LDKAKVLSLV AVQLHGNEDQ LYIDTLREAL
360 370 380 390 400
PAHVAIWKAL SVGETLPARE LQHVDKYVLD NGQGGSGQRF DWSLLNGQSL
410 420 430 440 450
GNVLLAGGLG ADNCVEAAQT GCAGLDFNSA VESQPGIKDA RLLASVFQTL

RAY
Length:453
Mass (Da):49,433
Last modified:March 19, 2014 - v3
Checksum:i7C30E71A58270033
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56554.1.
BA000007 Genomic DNA. Translation: BAB35257.1.
PIRiB90858.
F85761.
RefSeqiNP_287937.1. NC_002655.2.
NP_309861.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56554; AAG56554; Z2549.
BAB35257; BAB35257; BAB35257.
GeneIDi912854.
961398.
KEGGiece:Z2549.
ecs:ECs1834.
PATRICi18353731. VBIEscCol44059_2082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56554.1 .
BA000007 Genomic DNA. Translation: BAB35257.1 .
PIRi B90858.
F85761.
RefSeqi NP_287937.1. NC_002655.2.
NP_309861.1. NC_002695.1.

3D structure databases

ProteinModelPortali Q8X7B7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z2549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG56554 ; AAG56554 ; Z2549 .
BAB35257 ; BAB35257 ; BAB35257 .
GeneIDi 912854.
961398.
KEGGi ece:Z2549.
ecs:ECs1834.
PATRICi 18353731. VBIEscCol44059_2082.

Phylogenomic databases

eggNOGi COG0134.
HOGENOMi HOG000280458.
KOi K13498.
OMAi EKYFQGD.
OrthoDBi EOG6WT8JX.

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00042 .
UPA00035 ; UER00043 .
BioCyci ECOL386585:GJFA-1810-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
HAMAPi MF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProi IPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 2 hits.
PROSITEi PS00614. IGPS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiTRPC_ECO57
AccessioniPrimary (citable) accession number: Q8X7B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 19, 2014
Last modified: October 1, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3