Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P00929 (TRPA_SALTY)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tryptophan synthase alpha chain

Gene

trpA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.UniRule annotation

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
  2. Bifunctional protein TrpGD (trpGD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei49Proton acceptor1
Active sitei60Proton acceptor1

GO - Molecular functioni

Complete GO annotation...

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase alpha chainUniRule annotation (EC:4.2.1.20UniRule annotation)
Gene namesi
Name:trpAUniRule annotation
Ordered Locus Names:STM1727
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella ›
Proteomesi
  • UP000001014 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

DrugBankiDB07748. 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE.
DB07732. 2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE.
DB07745. 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE.
DB07894. 4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID.
DB07925. 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID.
DB07890. 4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID.
DB07773. 5-FLUOROINDOLE PROPANOL PHOSPHATE.
DB04143. Indole-3-Glycerol Phosphate.
DB03171. Indole-3-Propanol Phosphate.
DB07951. N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID.
DB07952. N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID.
DB07953. N-[1H-INDOL-3-YL-ACETYL]VALINE ACID.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000988391 – 268Tryptophan synthase alpha chainAdd BLAST268

Proteomic databases

PaxDbiP00929.
PRIDEiP00929.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
trpBP0A2K122EBI-1028423,EBI-1028431

Protein-protein interaction databases

DIPiDIP-1033N.
IntActiP00929. 1 interactor.
MINTiMINT-112862.
STRINGi99287.STM1727.

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 13Combined sources11
Beta strandi18 – 24Combined sources7
Turni25 – 28Combined sources4
Helixi30 – 42Combined sources13
Beta strandi46 – 51Combined sources6
Beta strandi58 – 60Combined sources3
Helixi62 – 73Combined sources12
Helixi78 – 91Combined sources14
Beta strandi93 – 95Combined sources3
Beta strandi97 – 101Combined sources5
Helixi103 – 107Combined sources5
Helixi111 – 121Combined sources11
Beta strandi125 – 128Combined sources4
Helixi133 – 135Combined sources3
Helixi137 – 145Combined sources9
Beta strandi149 – 151Combined sources3
Helixi160 – 169Combined sources10
Beta strandi174 – 181Combined sources8
Beta strandi185 – 187Combined sources3
Helixi194 – 202Combined sources9
Beta strandi208 – 213Combined sources6
Helixi217 – 225Combined sources9
Beta strandi229 – 233Combined sources5
Helixi235 – 243Combined sources9
Turni244 – 246Combined sources3
Helixi248 – 265Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A50X-ray2.30A1-268[»]
1A5AX-ray1.90A1-268[»]
1A5BX-ray2.00A1-268[»]
1A5SX-ray2.30A1-268[»]
1BEUX-ray1.90A1-268[»]
1BKSX-ray2.20A1-268[»]
1C29X-ray2.30A1-268[»]
1C8VX-ray2.20A1-268[»]
1C9DX-ray2.30A1-268[»]
1CW2X-ray2.00A1-268[»]
1CX9X-ray2.30A1-268[»]
1FUYX-ray2.25A1-268[»]
1K3UX-ray1.70A1-268[»]
1K7EX-ray2.30A1-268[»]
1K7FX-ray1.90A1-268[»]
1K7XX-ray1.70A1-268[»]
1K8XX-ray1.90A1-268[»]
1K8YX-ray1.50A1-268[»]
1K8ZX-ray1.70A1-268[»]
1KFBX-ray1.90A1-268[»]
1KFCX-ray1.50A1-268[»]
1KFEX-ray1.75A1-268[»]
1KFJX-ray1.80A1-268[»]
1KFKX-ray2.40A1-268[»]
1QOPX-ray1.40A1-268[»]
1QOQX-ray1.80A1-268[»]
1TJPX-ray1.50A1-268[»]
1TTPX-ray2.30A1-268[»]
1TTQX-ray2.00A1-268[»]
1UBSX-ray1.90A1-268[»]
1WBJX-ray1.50A1-268[»]
2CLEX-ray1.50A1-268[»]
2CLFX-ray1.70A1-268[»]
2CLHX-ray1.70A1-268[»]
2CLIX-ray1.70A1-268[»]
2CLKX-ray1.50A1-268[»]
2CLLX-ray1.60A1-268[»]
2CLMX-ray1.51A1-268[»]
2CLOX-ray1.50A1-268[»]
2J9XX-ray1.90A1-268[»]
2J9YX-ray1.80A1-268[»]
2J9ZX-ray1.80A1-268[»]
2RH9X-ray1.70A1-268[»]
2RHGX-ray2.00A1-268[»]
2TRSX-ray2.04A1-268[»]
2TSYX-ray2.50A1-268[»]
2TYSX-ray1.90A1-268[»]
2WSYX-ray3.05A1-268[»]
3CEPX-ray2.10A1-268[»]
3PR2X-ray1.85A2-267[»]
4HN4X-ray1.64A1-268[»]
4HPJX-ray1.45A1-268[»]
4HPXX-ray1.65A1-268[»]
4HT3X-ray1.30A1-268[»]
4KKXX-ray1.77A1-268[»]
4WX2X-ray1.75A1-268[»]
4XUGX-ray1.65A1-268[»]
4Y6GX-ray1.65A1-268[»]
4ZQCX-ray1.54A1-268[»]
5BW6X-ray1.82A1-268[»]
5CGQX-ray1.18A1-268[»]
ProteinModelPortaliP00929.
SMRiP00929.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00929.

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F6H. Bacteria.
COG0159. LUCA.
HOGENOMiHOG000223814.
KOiK01695.
OMAiDYPPEEC.
PhylomeDBiP00929.

Family and domain databases

CDDicd04724. Tryptophan_synthase_alpha. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
PfamiView protein in Pfam
PF00290. Trp_syntA. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiView protein in PROSITE
PS00167. TRP_SYNTHASE_ALPHA. 1 hit.

Sequencei

Sequence statusi: Complete.

P00929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL 
        60         70         80         90        100
GVPFSDPLAD GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL 
       110        120        130        140        150
MYANLVFNNG IDAFYARCEQ VGVDSVLVAD VPVEESAPFR QAALRHNIAP 
       160        170        180        190        200
IFICPPNADD DLLRQVASYG RGYTYLLSRS GVTGAENRGA LPLHHLIEKL 
       210        220        230        240        250
KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI IEKNLASPKQ 
       260 
MLAELRSFVS AMKAASRA
Length:268
Mass (Da):28,671
Last modified:July 21, 1986 - v1
Checksum:iF409BF1A931581B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01376 Genomic DNA. Translation: CAA24666.1.
J01810 Genomic DNA. Translation: AAA27235.1.
AE006468 Genomic DNA. Translation: AAL20645.1.
PIRiA93837. TSEBAT.
RefSeqiNP_460686.1. NC_003197.2.
WP_000443030.1. NC_003197.2.

Genome annotation databases

EnsemblBacteriaiAAL20645; AAL20645; STM1727.
GeneIDi1253246.
KEGGistm:STM1727.
PATRICifig|99287.12.peg.1823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01376 Genomic DNA. Translation: CAA24666.1.
J01810 Genomic DNA. Translation: AAA27235.1.
AE006468 Genomic DNA. Translation: AAL20645.1.
PIRiA93837. TSEBAT.
RefSeqiNP_460686.1. NC_003197.2.
WP_000443030.1. NC_003197.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A50X-ray2.30A1-268[»]
1A5AX-ray1.90A1-268[»]
1A5BX-ray2.00A1-268[»]
1A5SX-ray2.30A1-268[»]
1BEUX-ray1.90A1-268[»]
1BKSX-ray2.20A1-268[»]
1C29X-ray2.30A1-268[»]
1C8VX-ray2.20A1-268[»]
1C9DX-ray2.30A1-268[»]
1CW2X-ray2.00A1-268[»]
1CX9X-ray2.30A1-268[»]
1FUYX-ray2.25A1-268[»]
1K3UX-ray1.70A1-268[»]
1K7EX-ray2.30A1-268[»]
1K7FX-ray1.90A1-268[»]
1K7XX-ray1.70A1-268[»]
1K8XX-ray1.90A1-268[»]
1K8YX-ray1.50A1-268[»]
1K8ZX-ray1.70A1-268[»]
1KFBX-ray1.90A1-268[»]
1KFCX-ray1.50A1-268[»]
1KFEX-ray1.75A1-268[»]
1KFJX-ray1.80A1-268[»]
1KFKX-ray2.40A1-268[»]
1QOPX-ray1.40A1-268[»]
1QOQX-ray1.80A1-268[»]
1TJPX-ray1.50A1-268[»]
1TTPX-ray2.30A1-268[»]
1TTQX-ray2.00A1-268[»]
1UBSX-ray1.90A1-268[»]
1WBJX-ray1.50A1-268[»]
2CLEX-ray1.50A1-268[»]
2CLFX-ray1.70A1-268[»]
2CLHX-ray1.70A1-268[»]
2CLIX-ray1.70A1-268[»]
2CLKX-ray1.50A1-268[»]
2CLLX-ray1.60A1-268[»]
2CLMX-ray1.51A1-268[»]
2CLOX-ray1.50A1-268[»]
2J9XX-ray1.90A1-268[»]
2J9YX-ray1.80A1-268[»]
2J9ZX-ray1.80A1-268[»]
2RH9X-ray1.70A1-268[»]
2RHGX-ray2.00A1-268[»]
2TRSX-ray2.04A1-268[»]
2TSYX-ray2.50A1-268[»]
2TYSX-ray1.90A1-268[»]
2WSYX-ray3.05A1-268[»]
3CEPX-ray2.10A1-268[»]
3PR2X-ray1.85A2-267[»]
4HN4X-ray1.64A1-268[»]
4HPJX-ray1.45A1-268[»]
4HPXX-ray1.65A1-268[»]
4HT3X-ray1.30A1-268[»]
4KKXX-ray1.77A1-268[»]
4WX2X-ray1.75A1-268[»]
4XUGX-ray1.65A1-268[»]
4Y6GX-ray1.65A1-268[»]
4ZQCX-ray1.54A1-268[»]
5BW6X-ray1.82A1-268[»]
5CGQX-ray1.18A1-268[»]
ProteinModelPortaliP00929.
SMRiP00929.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-1033N.
IntActiP00929. 1 interactor.
MINTiMINT-112862.
STRINGi99287.STM1727.

Chemistry databases

DrugBankiDB07748. 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE.
DB07732. 2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE.
DB07745. 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE.
DB07894. 4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID.
DB07925. 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID.
DB07890. 4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID.
DB07773. 5-FLUOROINDOLE PROPANOL PHOSPHATE.
DB04143. Indole-3-Glycerol Phosphate.
DB03171. Indole-3-Propanol Phosphate.
DB07951. N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID.
DB07952. N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID.
DB07953. N-[1H-INDOL-3-YL-ACETYL]VALINE ACID.

Proteomic databases

PaxDbiP00929.
PRIDEiP00929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20645; AAL20645; STM1727.
GeneIDi1253246.
KEGGistm:STM1727.
PATRICifig|99287.12.peg.1823.

Phylogenomic databases

eggNOGiENOG4105F6H. Bacteria.
COG0159. LUCA.
HOGENOMiHOG000223814.
KOiK01695.
OMAiDYPPEEC.
PhylomeDBiP00929.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.

Miscellaneous databases

EvolutionaryTraceiP00929.

Family and domain databases

CDDicd04724. Tryptophan_synthase_alpha. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
PfamiView protein in Pfam
PF00290. Trp_syntA. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiView protein in PROSITE
PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTRPA_SALTY
AccessioniPrimary (citable) accession number: P00929
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 7, 2017
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.