Reviewed, UniProtKB/Swiss-Prot P06558 (TRPG_CORGL)

Names and origin

Protein names

Recommended name:
    Anthranilate synthase component 2
    EC=4.1.3.27
Alternative name(s):
    Anthranilate synthase component II
    Glutamine amido-transferase

Gene names

Name:	trpG
Ordered Locus Names:	Cgl3031, cg3360

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subunit structure	Tetramer of two components I and two components II.
Miscellaneous	Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Domain	Glutamine amidotransferase
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	anthranilate synthase 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 – 208	208	Anthranilate synthase component 2		PRO_0000056876
Regions
	Domain	3 – 208	206	Glutamine amidotransferase type-1
Sites
	Active site	80	1	By similarity
	Active site	185	1	By similarity
	Active site	187	1	By similarity
Experimental info
	Sequence conflict	133	1	I → V in CAA28624. Ref.1
	Sequence conflict	196	1	V → I in CAA28624. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P06558-1 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 6109497066EFA263	FASTA	208	21,875
	10 20 30 40 50 60 MTHVVLIDNH DSFVYNLVDA FAVAGYKCTV FRNTVPVETI LAANPDLICL SPGPGYPADA 70 80 90 100 110 120 GNMMALIERT LGQIPLLGIC LGYQALIEYH GGKVEPCGPV HGTTDNMILT DAGVQSPVFA 130 140 150 160 170 180 GLATDVEPDH PEIPGRKVPI GRYHSLGCVV APDGIESLGT CSSEIGDVIM AARTTDGKAI 190 200 GLQFHPESVL SPTGPVILSR CVEQLLAN

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. , 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: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X04960 Genomic DNA. Translation: CAA28624.1. BA000036 Genomic DNA. Translation: BAC00425.1. BX927157 Genomic DNA. Translation: CAF18971.1.
PIR	C24723.
RefSeq	NP_602224.1. YP_227281.1.
3D structure databases
HSSP	HSSP built from PDB template 1I1Q based on UniProtKB P00905.
ModBase	Search...
Genome annotation databases
GeneID	1020973. 3345522.
GenomeReviews	Gene locus Cgl3031 in contig BA000036_GR. Gene locus cg3360 in contig BX927147_GR.
KEGG	cgb:cg3360. cgl:NCgl2928.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P06558.
OMA	VVIYRND.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG3360-MON.
BRENDA	4.1.3.27. 812.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR006221. TrpG_papA. [Graphical view]
Pfam	PF00117. GATase. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00096. GATASE.
TIGRFAMs	TIGR00566. trpG_papA. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPG_CORGL

Accession

Primary (citable) accession number: P06558

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	July 11, 2002
Last modified:	November 3, 2009
This is version 78 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)