Reviewed, UniProtKB/Swiss-Prot P14952 (TRPG_CLOTM)

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

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	91 AA.
Sequence status	Fragment.
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
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 – ›91	›91	Anthranilate synthase component 2		PRO_0000056875
Regions
	Domain	4 – ›91	›88	Glutamine amidotransferase type-1
Sites
	Active site	82	1	By similarity
Experimental info
	Non-terminal residue	91	1

Sequences

	Sequence		Length	Mass (Da)
	P14952-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: E5718595500BF1AF	FASTA	91	10,272
	10 20 30 40 50 60 MIENILIIDN YDSFTYNLYQ YVGEISPNIE VYRNDKITLE KIEEMNPTHI IISPGPGFPK 70 80 90 DAGICIEAIR KFGRYIPILG VCLGHQAIGE A

References

[1]	"Molecular cloning and the nucleotide sequence of the Clostridium thermocellum trpE gene." Sato S., Nakada Y., Hon-Nami K., Yasui K., Shiratsuchi A. J. Biochem. 105:362-366(1989) [PubMed: 2732211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00399 Genomic DNA. Translation: BAA00301.1.
PIR	PT0065.
3D structure databases
HSSP	HSSP built from PDB template 1QDL based on UniProtKB Q06129.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.3.27. 97464.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view]
Pfam	PF00117. GATase. 1 hit. [Graphical view]
PRINTS	PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPG_CLOTM

Accession

Primary (citable) accession number: P14952

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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