Q08654 (TRPG_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthranilate synthase component II
EC=4.1.3.27

Including the following 2 domains:

1. Glutamine amidotransferase
2. Anthranilate phosphoribosyltransferase
   EC=2.4.2.18

Gene names

Name:	trpGD
Synonyms:	trpD
Ordered Locus Names:	TM_0141

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. HAMAP MF_00211 N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00211
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. HAMAP MF_00211 Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
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. HAMAP MF_00211
Sequence similarities	In the C-terminal section; belongs to the anthranilate phosphoribosyltransferase family. 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	Glycosyltransferase Lyase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference 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 phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC 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 – 589	589	Anthranilate synthase component II HAMAP MF_00211		PRO_0000056901
Regions
	Domain	46 – 241	196	Glutamine amidotransferase type-1
	Region	253 – 589	337	Anthranilate phosphoribosyltransferase HAMAP MF_00211
Sites
	Active site	126	1	For GATase activity By similarity
	Active site	215	1	For GATase activity By similarity
	Active site	217	1	For GATase activity By similarity
Experimental info
	Sequence conflict	384	1	E → G in CAA52203. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q08654 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 8DF80E6DA0C68610	FASTA	589	64,269
	10 20 30 40 50 60 MAPGRSGYRL RFRSGARISG DSEQTQGFVQ EPGSCAEDPG GIVLKRVIVI DNYDSFVYNI 70 80 90 100 110 120 VQYIGEVEPD CEIEVFRNDE ITIEEIERKN PTHIVISPGP GRPEEAGISV DVVRHFSGKV 130 140 150 160 170 180 PILGVCLGHQ VIGYAFGGKI VHAKRILHGK TSKIVHNGKG VFSGVKNPLV ATRYHSLVVE 190 200 210 220 230 240 EASLPEVLEI TAKSDDGEIM GLQHKEHPTF GVQFHPESVL TEEGKRIIKN FLNIQDIQVK 250 260 270 280 290 300 KVSEETEIDI VSALKKLVEF EDLTFEESRQ VMNFIMSGNA TDAQIAGFLV ALRMKEETGD 310 320 330 340 350 360 ELGGMASVMR EKSIHIKAPS PRTVDTCGTG GDGFGTFNIS TTTAFVVAAA GIPVAKHGNR 370 380 390 400 410 420 SVSSKVGSAD VLEAGGYKLE KTPEEMEREL KETGFSFLFA PLLHPAMKHV MPARRQLKIR 430 440 450 460 470 480 TAFNLLGPIT NPARVKYQVV GVFDLSFASK LATALQRLGT ERSAVVNGGF TDELTTCGKN 490 500 510 520 530 540 NLLLVTQEEI VPMVLDPEEL GLKSGDPEEL KGPSDPKEAY RMMESVLKGE ASRTQVETVA 550 560 570 580 LNAGVVFWLV GECDTIKDGV GKALDLIRTG EAYKKLREVM DYQKTLGNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries. Identification and sequencing of the trpEG (D) operon." Kim C.W., Markiewicz P.G., Lee J.J., Schierle C.F., Miller J.H. J. Mol. Biol. 231:960-981(1993) [PubMed: 7685830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]	"(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima." Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K. EMBO J. 14:4395-4402(1995) [PubMed: 7556082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-589.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74075 Genomic DNA. Translation: CAA52203.1. AE000512 Genomic DNA. Translation: AAD35234.1. X92729 Genomic DNA. Translation: CAA63388.1.
PIR	C72414.
RefSeq	NP_227956.1. NC_000853.1.
3D structure databases
ProteinModelPortal	Q08654.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	896971.
GenomeReviews	Gene locus TM_0141 in contig AE000512_GR.
KEGG	tma:TM0141.
NMPDR	fig|243274.1.peg.140.
PATRIC	23935124. VBITheMar51294_0140.
TIGR	TM_0141.
Phylogenomic databases
HOGENOM	HBG559996.
OMA	NAMFALY.
PhylomeDB	Q08654.
ProtClustDB	PRK14607.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-282. TMAR243274:TM_0141-MONOMER.
Family and domain databases
HAMAP	MF_00211. TrpD. Fused. [Tree]
InterPro	IPR005940. Anthranilate_Pribosyl_Tfrase. IPR017926. GATASE_1. IPR000312. Glycosyl_Trfase_fam3. IPR017459. Glycosyl_Trfase_fam3_N. IPR020072. Glycosyl_Trfase_fam3_subgr_N. IPR006221. TrpG_papA. [Graphical view]
Gene3D	G3DSA:1.20.970.10. Glyco_trans_3. 2 hits. G3DSA:3.40.1030.10. Glyco_trans_3. 2 hits.
KO	K13497.
Pfam	PF00117. GATase. 1 hit. PF02885. Glycos_trans_3N. 1 hit. PF00591. Glycos_transf_3. 1 hit. [Graphical view]
SUPFAM	SSF47648. Glyco_trans_3. 1 hit. SSF52418. Glyco_trans_3. 1 hit.
TIGRFAMs	TIGR01245. TrpD. 1 hit. TIGR00566. TrpG_papA. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPG_THEMA

Accession

Primary (citable) accession number: Q08654

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
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