Reviewed, UniProtKB/Swiss-Prot P00905 (TRPG_SALTY)

Names and origin

Protein names

Recommended name:
    Anthranilate synthase component II
    EC=4.1.3.27
Including the following 2 domains:
    1- Recommended name:
            Glutamine amidotransferase
    2- Recommended name:
            Anthranilate phosphoribosyltransferase
              EC=2.4.2.18

Gene names

Name:	trpD
Synonyms:	trpGD
Ordered Locus Names:	STM1724

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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	Contains 2 chains with different activities: 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	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tryptophan biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	anthranilate phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP anthranilate synthase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpE	P00898	1	EBI-1030724,EBI-1030716

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 531

530

Anthranilate synthase component II HAMAP MF_00211

PRO_0000056897

Regions

Domain

3 – 196

194

Glutamine amidotransferase type-1

Region

202 – 531

330

Anthranilate phosphoribosyltransferase HAMAP MF_00211

Sites

Active site

84

1

For GATase activity By similarity

Active site

170

1

For GATase activity By similarity

Active site

172

1

For GATase activity By similarity

Experimental info

Sequence conflict

191 – 192

2

QQ → LA in AAA57312. Ref.3

Sequence conflict

511

1

V → L in AAA27236. Ref.1

Secondary structure

1

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531

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

14 – 23

10

Beta strand

27 – 32

6

Helix

38 – 44

7

Beta strand

48 – 54

7

Helix

61 – 63

3

Helix

67 – 74

8

Beta strand

80 – 83

4

Helix

85 – 93

9

Beta strand

106 – 114

9

Helix

118 – 120

3

Beta strand

125 – 131

7

Beta strand

145 – 150

6

Beta strand

153 – 159

7

Turn

160 – 163

4

Beta strand

164 – 170

7

Helix

179 – 190

12

Sequences

	Sequence		Length	Mass (Da)
	P00905-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 256D2409062CD4C7	FASTA	531	56,918
	10 20 30 40 50 60 MADILLLDNI DSFTWNLADQ LRTNGHNVVI YRNHIPAQTL IDRLATMKNP VLMLSPGPGV 70 80 90 100 110 120 PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF 130 140 150 160 170 180 AGLANPLPVA RYHSLVGSNV PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA 190 200 210 220 230 240 RLLEQTLAWA QQKLEPTNTL QPILEKLYQA QTLTQQESHQ LFSAVVRGEL KPEQLAAALV 250 260 270 280 290 300 SMKIRGEHPN EIAGAATALL ENAAPFPRPE YLFADIVGTG GDGSNSINIS TASAFVAAAC 310 320 330 340 350 360 GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGLRHA 370 380 390 400 410 420 MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG 430 440 450 460 470 480 MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQDQL AGGTPEENRD ILTRLLQGKG 490 500 510 520 530 DAAHEAAVAA NVAMLMRLHG QEDLKANAQT VLDVLRNGTA YDRVTALAAR G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium." Horowitz H., van Arsdell J., Platt T. J. Mol. Biol. 169:775-797(1983) [PubMed: 6355484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens." Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C. J. Mol. Biol. 142:503-517(1980) [PubMed: 7007652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M30285 Genomic DNA. Translation: AAA27236.1.
AE008776 Genomic DNA. Translation: AAL20642.1.
J01811 Genomic DNA. Translation: AAA57312.1.

PIR

NNEB2T. A92907.

RefSeq

NP_460683.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I1Q	X-ray	1.90	B	2-192	[»]

SMR

P00905. Positions 199-530.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00905. 1 interaction.

Genome annotation databases

GeneID

1253243.

GenomeReviews

Gene locus STM1724 in contig AE006468_GR.

KEGG

stm:STM1724.

NMPDR

fig|99287.1.peg.1670.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P00905.

OMA

P00905. ILSPGPK.

Enzyme and pathway databases

BioCyc

STYP99287:STM1724-MON.

BRENDA

2.4.2.18. 2.
4.1.3.27. 2.

Family and domain databases

HAMAP

MF_00211. Fused.
[Tree]

InterPro

IPR005940. Ant_phspho_trans.
IPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N.
IPR006221. TrpG_papA.
[Graphical view]

Gene3D

G3DSA:3.40.1030.10. Glyco_trans_3. 1 hit.

Pfam

PF00117. GATase. 1 hit.
PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]

PRINTS

PR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.

ProDom

PD001864. Glyco_trans_3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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_SALTY

Accession

Primary (citable) accession number: P00905

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 98 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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