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P00897

- TRPE_SERMA

UniProt

P00897 - TRPE_SERMA

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Protein
Anthranilate synthase component 1
Gene
trpE
Organism
Serratia marcescens
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia Inferred.1 Publication

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Cofactori

Binds 1 magnesium ion per subunit.1 Publication

Enzyme regulationi

Feedback inhibited by tryptophan By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Tryptophan
Metal bindingi360 – 3601Magnesium
Binding sitei448 – 4481Substrate
Binding sitei468 – 4681Substrate
Binding sitei484 – 4841Substrate; via amide nitrogen
Metal bindingi497 – 4971Magnesium

GO - Molecular functioni

  1. anthranilate synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. tryptophan biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase component 1 (EC:4.1.3.27)
Short name:
AS
Short name:
ASI
Gene namesi
Name:trpE
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Anthranilate synthase component 1
PRO_0000154111Add
BLAST

Proteomic databases

PRIDEiP00897.

Interactioni

Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
trpGP009002EBI-1031345,EBI-1031352

Protein-protein interaction databases

IntActiP00897. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147
Helixi20 – 289
Beta strandi32 – 409
Turni42 – 443
Beta strandi47 – 6317
Beta strandi66 – 716
Helixi76 – 783
Helixi79 – 868
Beta strandi91 – 966
Beta strandi99 – 1035
Beta strandi109 – 1113
Helixi113 – 1175
Helixi123 – 1308
Beta strandi132 – 1343
Beta strandi142 – 1498
Helixi151 – 1566
Beta strandi171 – 18414
Turni185 – 1884
Beta strandi189 – 1968
Helixi201 – 21818
Beta strandi236 – 2394
Helixi241 – 25616
Beta strandi261 – 2633
Beta strandi266 – 2727
Helixi277 – 28610
Beta strandi290 – 2967
Beta strandi301 – 3077
Beta strandi309 – 3146
Turni315 – 3184
Beta strandi319 – 3224
Beta strandi325 – 3295
Helixi341 – 35313
Helixi355 – 37521
Turni378 – 3803
Beta strandi382 – 39110
Beta strandi396 – 40611
Helixi412 – 4198
Helixi423 – 4253
Beta strandi426 – 4294
Helixi430 – 44112
Turni446 – 4494
Beta strandi450 – 4567
Beta strandi461 – 4655
Beta strandi468 – 4736
Beta strandi476 – 4827
Helixi491 – 51222

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7QX-ray1.95A/C1-519[»]
1I7SX-ray2.40A/C1-519[»]
ProteinModelPortaliP00897.
SMRiP00897. Positions 3-519.

Miscellaneous databases

EvolutionaryTraceiP00897.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 2923Tryptophan binding
Regioni327 – 3282Substrate binding
Regioni482 – 4843Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I_like.
IPR006805. Anth_synth_I_N.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate-bd_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF001373. TrpE. 1 hit.
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00565. trpE_proteo. 1 hit.

Sequencei

Sequence statusi: Complete.

P00897-1 [UniParc]FASTAAdd to Basket

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MNTKPQLTLL KVQASYRGDP TTLFHQLCGA RPATLLLESA EINDKQNLQS    50
LLVIDSALPI TALGHTVSVQ ALTANGPALL PVLDEALPPE VRNQARPNGR 100
ELTFPAIDAV QDEDARLRSL SVFDALRTLL TLVDSPADER EAVMLGGLFA 150
YDLVAGFENL PAVRQDQRCP DFCFYLAETL LVLDHQRGSA RLQASVFSEQ 200
ASEAQRLQHR LEQLQAELQQ PPQPIPHQKL ENMQLSCNQS DEEYGAVVSE 250
LQEAIRQGEI FQVVPSRRFS LPCPAPLGPY QTLKDNNPSP YMFFMQDDDF 300
TLFGASPESA LKYDAGNRQI EIYPIAGTRP RGRRADGSLD LDLDSRIELE 350
MRTDHKELAE HLMLVDLARN DLARICQAGS RYVADLTKVD RYSFVMHLVS 400
RVVGTLRADL DVLHAYQACM NMGTLSGAPK VRAMQLIAAL RSTRRGSYGG 450
RVGYFTAHRH LDTCIVIRSA YVEDGHRTVQ AGAGVVQDSI RRREADETRN 500
KARAVLRAIA TAHHAKEVF 519
Length:519
Mass (Da):57,658
Last modified:August 14, 2001 - v2
Checksum:iD3B59D47619FB0C1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti502 – 5043ARA → PVP in AAA57308. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY027546 Genomic DNA. Translation: AAA57308.2.
PIRiA01117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY027546 Genomic DNA. Translation: AAA57308.2 .
PIRi A01117.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I7Q X-ray 1.95 A/C 1-519 [» ]
1I7S X-ray 2.40 A/C 1-519 [» ]
ProteinModelPortali P00897.
SMRi P00897. Positions 3-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00897. 1 interaction.

Proteomic databases

PRIDEi P00897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00040 .

Miscellaneous databases

EvolutionaryTracei P00897.

Family and domain databases

Gene3Di 3.60.120.10. 1 hit.
InterProi IPR005801. ADC_synthase.
IPR019999. Anth_synth_I_like.
IPR006805. Anth_synth_I_N.
IPR005257. Anth_synth_I_TrpE.
IPR015890. Chorismate-bd_C.
[Graphical view ]
Pfami PF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view ]
PIRSFi PIRSF001373. TrpE. 1 hit.
PRINTSi PR00095. ANTSNTHASEI.
SUPFAMi SSF56322. SSF56322. 1 hit.
TIGRFAMsi TIGR00565. trpE_proteo. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan."
    Spraggon G., Kim C., Nguyen-Huu X., Yee M.-C., Yanofsky C., Mills S.E.
    Proc. Natl. Acad. Sci. U.S.A. 98:6021-6026(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND MAGNESIUM ION, FUNCTION, COFACTOR, SUBUNIT.
  2. "Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation."
    Li S.-L., Hanlon J., Yanofsky C.
    Biochemistry 13:1736-1744(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
    Strain: SM6.
  3. "The regulatory region of the trp operon of Serratia marcescens."
    Miozzari G.F., Yanofsky C.
    Nature 276:684-689(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
  4. "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] OF 494-519.
    Strain: SM6.

Entry informationi

Entry nameiTRPE_SERMA
AccessioniPrimary (citable) accession number: P00897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 14, 2001
Last modified: June 11, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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