Indole-3-glycerol phosphate synthase
     (IGPS)
     (EC 4.1.1.48)
N-(5'-phospho-ribosyl)anthranilate isomerase
     (PRAI)
     (EC 5.3.1.24)

Gene name

	Name:	trpC
	Synonyms:	trpCF
	OrderedLocusNames:	Cgl3033, cg3362

From

Corynebacterium glutamicum (Brevibacterium flavum)

[TaxID: 1718]

[HAMAP proteome]

Taxonomy

Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/14.24.10113; PubMed=3808947 [NCBI, ExPASy, EBI, Israel, Japan] Matsui K., Sano K., Ohtsubo E.; "Complete nucleotide and deduced amino acid sequences of the Brevibacterium lactofermentum tryptophan operon."; Nucleic Acids Res. 14:10113-10114(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).

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.
CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO₂ + H₂O.
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5 .
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5 .
SUBUNIT: Monomer.
SIMILARITY: In the N-terminal section; belongs to the trpC family.
SIMILARITY: In the C-terminal section; belongs to the trpF family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X04960; CAA28626.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAC00427.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927157; CAF18973.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E24723; E24723.

RefSeq

NP_602226.2; -.
YP_227283.1; -.

3D structure databases

HSSP

P00909; 1JCM. [HSSP ENTRY / PDB]

ModBase

P06560.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG3362-MON; -.

Ontologies

GO:0004425;	Molecular function: indole-3-glycerol-phosphate synthase activity (inferred from electronic annotation from HAMAP).
GO:0004640;	Molecular function: phosphoribosylanthranilate isomerase activity (inferred from electronic annotation from HAMAP).
GO:0000162;	Biological process: tryptophan biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00134; fused; 1.
MF_00135; fused; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR013798; Indole-3-GPS.
IPR001468; Indole-3-GPS_central.
IPR001240; PRAI.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00218; IGPS; 1.
PF00697; PRAI; 1.
Pfam graphical view of domain structure.

ProDom

PD001511; IGPS; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00614; IGPS; 1.

Genome annotation databases

GeneID

1020975; -.
3345646; -.

GenomeReviews

BA000036_GR; Cgl3033.
BX927147_GR; cg3362.

KEGG

cgb:cg3362; -.

Phylogenomic databases

HOGENOM

P06560; -.

Genome annotation databases

CMR

P06560; Cgl3033.

Other

ProtoNet

P06560.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Decarboxylase; Isomerase; Lyase; Multifunctional enzyme; Tryptophan biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 474`	`474`	`Tryptophan biosynthesis protein trpCF.`	`PRO_0000154276`
`REGION`	`1 262`	`262`	`Indole-3-glycerol phosphate synthase.`
`REGION`	`263 474`	`212`	`N-(5'-phosphoribosyl)anthranilate isomerase.`
`CONFLICT`	`88 89`		`SG -> AA (in Ref. 1; CAA28626).`
`CONFLICT`	`110 110`		`A -> G (in Ref. 1; CAA28626).`
`CONFLICT`	`130 131`		`HA -> RP (in Ref. 1; CAA28626).`
`CONFLICT`	`153 153`		`A -> D (in Ref. 1; CAA28626).`
`CONFLICT`	`302 302`		`L -> S (in Ref. 1; CAA28626).`
`CONFLICT`	`343 343`		`D -> G (in Ref. 1; CAA28626).`
`CONFLICT`	`381 383`		`Missing (in Ref. 1; CAA28626).`
`CONFLICT`	`454 474`		`AGAKDAGALLKIFATISTFHY -> GWGERCRRAAENFRDHLHIPLLKV (in Ref. 1; CAA28626).`

Sequence information

Length: 474 AA [This is the length of the unprocessed precursor]

Molecular weight: 50477 Da [This is the MW of the unprocessed precursor]

CRC64: C347C7016BB97F9A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSNNLPTVL ESIVEGRRGH LEEIRARIAH VDVDALPKST RSLFDSLNQG RGGARFIMEC 

        70         80         90        100        110        120 
KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG GDYDHLATVA ATSHLPVLCK 

       130        140        150        160        170        180 
DFIIDPVQVH AARYFGADAI LLMLSVLDDE EYAALAAEAA RFDLDILTEV IDEEEVARAI 

       190        200        210        220        230        240 
KLGAKIFGVN HRNLHDLSID LDRSRRLSKL IPADAVLVSE SGVRDTETVR QLGGHSNAFL 

       250        260        270        280        290        300 
VGSQLTSQEN VDLAARELVY GPNKVCGLTS PSAAQTARAA GAVYGGLIFE EASPRNVSRE 

       310        320        330        340        350        360 
TLQKIIAAEP NLRYVAVSRR TSGYKDLLVD GIFAVQIHAP LQDSVEAEKA LIAAVREEVG 

       370        380        390        400        410        420 
PQVQVWRAIS MSSPLGAEVA AAVEGDVDKL ILDAHEGGSG EVFDWATVPA AVKAKSLLAG 

       430        440        450        460        470 
GISPDNAAQA LAVGCAGLDI NSGVEYPAGA GTWAGAKDAG ALLKIFATIS TFHY

P06560 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools