P06560 (TRPC_CORGL) 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
Synonyms:	trpCF
Ordered Locus Names:	Cgl3033, cg3362

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	474 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.
Sequence similarities	In the N-terminal section; belongs to the TrpC family. In the C-terminal section; belongs to the TrpF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Isomerase Lyase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
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 – 474	474	Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B		PRO_0000154276
Regions
	Region	1 – 262	262	Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
	Region	263 – 474	212	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B
Experimental info
	Sequence conflict	88 – 89	2	SG → AA in CAA28626. Ref.1
	Sequence conflict	110	1	A → G in CAA28626. Ref.1
	Sequence conflict	130 – 131	2	HA → RP in CAA28626. Ref.1
	Sequence conflict	153	1	A → D in CAA28626. Ref.1
	Sequence conflict	302	1	L → S in CAA28626. Ref.1
	Sequence conflict	343	1	D → G in CAA28626. Ref.1
	Sequence conflict	381 – 383	3	Missing in CAA28626. Ref.1
	Sequence conflict	454 – 474	21	AGAKD…STFHY → GWGERCRRAAENFRDHLHIP LLKV in CAA28626. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P06560 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: C347C7016BB97F9A	FASTA	474	50,477
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide and deduced amino acid sequences of the Brevibacterium lactofermentum tryptophan operon." Matsui K., Sano K., Ohtsubo E. Nucleic Acids Res. 14:10113-10114(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." 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. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04960 Genomic DNA. Translation: CAA28626.1. BA000036 Genomic DNA. Translation: BAC00427.1. BX927157 Genomic DNA. Translation: CAF18973.1.
PIR	E24723.
RefSeq	NP_602226.2. NC_003450.3. YP_227283.1. NC_006958.1.
3D structure databases
ProteinModelPortal	P06560.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg3362.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC00427; BAC00427; BAC00427. CAF18973; CAF18973; cg3362.
GeneID	1020975. 3345646.
KEGG	cgb:cg3362. cgl:NCgl2930.
PATRIC	21498118. VBICorGlu203724_2967.
Phylogenomic databases
eggNOG	COG0134.
KO	K13498.
OMA	YILECKK.
ProtClustDB	PRK09427.
Enzyme and pathway databases
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_dom. 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_CORGL

Accession

Primary (citable) accession number: P06560

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	July 26, 2002
Last modified:	May 29, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program