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P00906

- TRPG_SHIDY

UniProt

P00906 - TRPG_SHIDY

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Protein
Anthranilate synthase component II
Gene
trpG-TRPD
Organism
Shigella dysenteriae
Status
Reviewed - Annotation score: 4 out of 5 - Protein predictedi

Functioni

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841For GATase activity By similarity
Active sitei170 – 1701For GATase activity By similarity
Active sitei172 – 1721For GATase activity By similarity

GO - Molecular functioni

  1. anthranilate phosphoribosyltransferase activity Source: UniProtKB-EC
  2. anthranilate synthase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB-KW
  2. tryptophan biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.

Names & Taxonomyi

Protein namesi
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 namesi
Name:trpG-TRPD
OrganismiShigella dysenteriae
Taxonomic identifieri622 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – ›201›200Anthranilate synthase component II
PRO_0000056899Add
BLAST

Interactioni

Subunit structurei

Tetramer of two components I and two components II.

Structurei

3D structure databases

ProteinModelPortaliP00906.
SMRiP00906. Positions 2-193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 196194Glutamine amidotransferase type-1
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00906-1 [UniParc]FASTAAdd to Basket

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MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP    50
VLMLSPGPGV PSEAGCMPEL LTRLSGKLPI IGICLGHQAI VEAYGGYVGQ 100
AGEILHGKAS SIEHDGQAMF AGLTNPLPVA RYHSLVGSNI PAGLTINAHF 150
NGMVMAVRHD ADRICGFQFH PESILTTQGA RLLEQTLAWA QRKLEPTNTL 200
Q 201
Length:201
Mass (Da):21,700
Last modified:January 23, 2007 - v2
Checksum:i943E3DBE4F0E59AF
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei201 – 2011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01787 Genomic DNA. Translation: AAA57307.1.
PIRiB92860. NNEB2D.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01787 Genomic DNA. Translation: AAA57307.1 .
PIRi B92860. NNEB2D.

3D structure databases

ProteinModelPortali P00906.
SMRi P00906. Positions 2-193.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00040 .
UPA00035 ; UER00041 .

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view ]
Pfami PF00117. GATase. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR00566. trpG_papA. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiTRPG_SHIDY
AccessioniPrimary (citable) accession number: P00906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
In E.coli and certain other bacteria, component II is larger and its C-terminal two thirds has anthranilate phosphoribosyltransferase activity.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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