Anthranilate synthase component II - Escherichia coli (strain K12)

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P00904 (TRPG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Anthranilate synthase component II
EC=4.1.3.27

Including the following 2 domains:

Glutamine amidotransferase
Anthranilate phosphoribosyltransferase
EC=2.4.2.18

Gene names

Name:	trpD
Synonyms:	trpGD
Ordered Locus Names:	b1263, JW1255

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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-Rule MF_00211 N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00211
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. HAMAP-Rule 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-Rule 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 Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tryptophan biosynthetic process Inferred from direct assay PubMed 2428387 PubMed 4886289. Source: EcoCyc
Molecular_function	anthranilate phosphoribosyltransferase activity Inferred from direct assay PubMed 2428387. Source: EcoCyc anthranilate synthase activity Inferred from direct assay PubMed 4886289. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 531

530

Anthranilate synthase component II HAMAP-Rule MF_00211

PRO_0000056877

Regions

Domain

3 – 196

194

Glutamine amidotransferase type-1

Region

202 – 531

330

Anthranilate phosphoribosyltransferase HAMAP-Rule MF_00211

Sites

Active site

For GATase activity By similarity

Active site

170

For GATase activity By similarity

Active site

172

For GATase activity By similarity

Experimental info

Sequence conflict

P → A Ref.2

Sequence conflict

192

Q → H Ref.1

Sequence conflict

192

Q → H Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P00904 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 10B02E455194F072
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FASTA

531

56,870

        10         20         30         40         50         60 
MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP VLMLSPGPGV 

        70         80         90        100        110        120 
PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF 

       130        140        150        160        170        180 
AGLTNPLPVA RYHSLVGSNI PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA 

       190        200        210        220        230        240 
RLLEQTLAWA QQKLEPANTL QPILEKLYQA QTLSQQESHQ LFSAVVRGEL KPEQLAAALV 

       250        260        270        280        290        300 
SMKIRGEHPN EIAGAATALL ENAAPFPRPD YLFADIVGTG GDGSNSINIS TASAFVAAAC 

       310        320        330        340        350        360 
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGFRHA 

       370        380        390        400        410        420 
MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG 

       430        440        450        460        470        480 
MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQEQL AGGTPEENRD ILTRLLQGKG 

       490        500        510        520        530 
DAAHEAAVAA NVAMLMRLHG HEDLQANAQT VLEVLRSGSA YDRVTALAAR G

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M. Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli." Horowitz H., Christie G.E., Platt T. J. Mol. Biol. 156:245-256(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Structural homology of the glutamine amidotransferase subunits of the anthranilate synthetases of Escherichia coli, Salmonella typhimurium and Serratia marcescens." Li S.-L., Hanlon J., Yanofsky C. Nature 248:48-50(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-62.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V00367 Genomic DNA. Translation: CAA23665.1. V00372 Genomic DNA. Translation: CAA23672.1. J01714 Genomic DNA. Translation: AAA57298.1. U00096 Genomic DNA. Translation: AAC74345.1. AP009048 Genomic DNA. Translation: BAA14798.1.
PIR	NNEC2. B64874.
RefSeq	NP_415779.1. NC_000913.2. YP_489531.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P00904.
SMR	P00904. Positions 2-193, 199-530.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1263.
Protein family/group databases
MEROPS	C26.960.
2D gel databases
SWISS-2DPAGE	P00904.
Proteomic databases
PaxDb	P00904.
PRIDE	P00904.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74345; AAC74345; b1263. BAA14798; BAA14798; BAA14798.
GeneID	12931129. 945109.
KEGG	ecj:Y75_p1237. eco:b1263.
PATRIC	32117786. VBIEscCol129921_1313.
Organism-specific databases
EchoBASE	EB1020.
EcoGene	EG11027. trpD.
Phylogenomic databases
eggNOG	COG0547.
HOGENOM	HOG000230451.
KO	K13497.
OMA	GPKHPKD.
ProtClustDB	PRK09522.
Enzyme and pathway databases
BioCyc	EcoCyc:ANTHRANSYNCOMPII-MONOMER. ECOL316407:JW1255-MONOMER. MetaCyc:ANTHRANSYNCOMPII-MONOMER.
UniPathway	UPA00035; UER00040. UPA00035; UER00041.
Gene expression databases
Genevestigator	P00904.
Family and domain databases
Gene3D	3.40.1030.10. 1 hit.
HAMAP	MF_00211. TrpD. Fused.
InterPro	IPR005940. Anthranilate_Pribosyl_Tfrase. IPR017926. GATASE_1. IPR000312. Glycosyl_Trfase_fam3. IPR017459. Glycosyl_Trfase_fam3_N_dom. IPR006221. TrpG/PapA. [Graphical view]
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_ECOLI

Accession

Primary (citable) accession number: P00904
Secondary accession number(s): P76833, P76835, P78302

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents