Q8X7B7 (TRPC_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Z2549, ECs1834

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Inferred 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 caution	The sequence AAG56554.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB35257.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Isomerase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	indole-3-glycerol-phosphate synthase activity Inferred from electronic annotation. Source: EC phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B		PRO_0000154278
Regions
	Region	1 – 256	256	Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
	Region	257 – 452	196	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

	Sequence		Length	Mass (Da)
	Q8X7B7 [UniParc]. Last modified March 25, 2003. Version 2. Checksum: DB4B5D8B556FF7A8	FASTA	452	49,302
	10 20 30 40 50 60 MQTVLAKIVA DKAIWVEARK QQQPLASFQN EVQPSTRHFY DALQGARTAF ILECKKASPS 70 80 90 100 110 120 KGVICDDFDP ARIAAIYKHY ASAISVLTDE KYFQGSFDFL PIVSQIAPQP ILCKDFIIDP 130 140 150 160 170 180 YQIYLARYYQ ADACLLMLSV LDDEQYRQLA AVAHSLKMGV LTEVSNEEEL ERAIALGAKV 190 200 210 220 230 240 VGINNRDLRD LSIDLNRTRE LAPKLGHNVT VISESGINTY AQVRELSHFA DGFLIGSALM 250 260 270 280 290 300 AHDDLHAAVR RVLLGENKVC GLTRGQDAKA AYDAGAIYGG LIFVATSPRC VNVEQAQEVM 310 320 330 340 350 360 AAAPLQYVGV FRNHDIADVL DKAKVLSLVA VQLHGNEDQL YIDTLREALP AHVAIWKALS 370 380 390 400 410 420 VGETLPAREL QHVDKYVLDN GQGGSGQRFD WSLLNGQSLG NVLLAGGLGA DNCVEAAQTG 430 440 450 CAGLDFNSAV ESQPGIKDAR LLASVFQTLR AY

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56554.1. Different initiation. BA000007 Genomic DNA. Translation: BAB35257.1. Different initiation.
PIR	B90858. F85761.
RefSeq	NP_287937.1. NC_002655.2. NP_309861.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X7B7.
SMR	Q8X7B7. Positions 1-452.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z2549.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG56554; AAG56554; Z2549. BAB35257; BAB35257; BAB35257.
GeneID	912854. 961398.
KEGG	ece:Z2549. ecs:ECs1834.
PATRIC	18353731. VBIEscCol44059_2082.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0134.
HOGENOM	HOG000280458.
KO	K13498.
OMA	YILECKK.
ProtClustDB	PRK09427.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-1810-MONOMER.
UniPathway	UPA00035; UER00042. UPA00035; UER00043.
Family and domain databases
Gene3D	3.20.20.70. 2 hits.
HAMAP	MF_00134_B. IGPS_B. Fused. MF_00135. PRAI. Fused.
InterPro	IPR013785. Aldolase_TIM. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GlycerolPSynthase_CS. IPR001240. PRAI. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Pfam	PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 2 hits.
PROSITE	PS00614. IGPS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPC_ECO57

Accession

Primary (citable) accession number: Q8X7B7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 25, 2003
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program