Tryptophan biosynthesis protein trpCF - Corynebacterium glutamicum

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Reviewed, UniProtKB/Swiss-Prot P06560 (TRPC_CORGL)

Last modified June 16, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Tryptophan biosynthesis protein trpCF
Including the following 2 domains:
    1- Recommended name:
            Indole-3-glycerol phosphate synthase
                Short name=IGPS
              EC=4.1.1.48
    2- Recommended name:
            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 (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

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Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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. HAMAP MF_00134
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP MF_00134 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO₂ + H₂O. HAMAP MF_00134
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP MF_00134 Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer. HAMAP MF_00134
Sequence similarities	In the N-terminal section; belongs to the trpC family. In the C-terminal section; belongs to the trpF family.

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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: HAMAP
Molecular function	indole-3-glycerol-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 474

474

Tryptophan biosynthesis protein trpCF HAMAP MF_00134

PRO_0000154276

Regions

Region

1 – 262

262

Indole-3-glycerol phosphate synthase HAMAP MF_00134

Region

263 – 474

212

N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Experimental info

Sequence conflict

88 – 89

SG → AA in CAA28626. Ref.1

Sequence conflict

110

A → G in CAA28626. Ref.1

Sequence conflict

130 – 131

HA → RP in CAA28626. Ref.1

Sequence conflict

153

A → D in CAA28626. Ref.1

Sequence conflict

302

L → S in CAA28626. Ref.1

Sequence conflict

343

D → G in CAA28626. Ref.1

Sequence conflict

381 – 383

Missing in CAA28626. Ref.1

Sequence conflict

454 – 474

AGAKD…STFHY → GWGERCRRAAENFRDHLHIP LLKV in CAA28626. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P06560-1 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: C347C7016BB97F9A
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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

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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: 3808947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases 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. Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

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Cross-references

Sequence databases
	X04960 Genomic DNA. Translation: CAA28626.1. BA000036 Genomic DNA. Translation: BAC00427.1. BX927157 Genomic DNA. Translation: CAF18973.1.
PIR	E24723.
RefSeq	NP_602226.2. YP_227283.1.
3D structure databases
HSSP	HSSP built from PDB template 1JCM based on UniProtKB P00909.
ModBase	Search...
Genome annotation databases
GeneID	1020975. 3345646.
GenomeReviews	Gene locus Cgl3033 in contig BA000036_GR. Gene locus cg3362 in contig BX927147_GR.
KEGG	cgb:cg3362.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P06560.
OMA	P06560. YILECKK.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG3362-MON.
BRENDA	4.1.1.48. 812. 5.3.1.24. 812.
Family and domain databases
HAMAP	MF_00134. Fused. [Tree] MF_00135. Fused. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GPS_central. IPR001240. PRAI. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
ProDom	PD001511. IGPS. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00614. IGPS. 1 hit. [Graphical view]
ProtoNet	Search...

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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:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents