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Protein

Tryptophan synthase alpha chain

Gene

trpA

Organism
Shewanella frigidimarina
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotationSAAS annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton acceptorUniRule annotation
Active sitei61 – 611Proton acceptorUniRule annotation

GO - Molecular functioni

  1. tryptophan synthase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesisUniRule annotationSAAS annotation

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 annotationImported
OrganismiShewanella frigidimarinaImported
Taxonomic identifieri56812 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.UniRule annotationSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VNDX-ray2.60A/B/C/D/E/F/G/H1-267[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpA family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha.
InterProiIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamiPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

H1AFK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNRYQAKFA ALKAQDKGAF VPFVTIGDPS PELSLKIIQT LVDNGADALE
60 70 80 90 100
LGFPFSDPLA DGPVIQGANL RSLAAGTTSS DCFDIITKVR AQHPDMPIGL
110 120 130 140 150
LLYANLVFAN GIDEFYTKAQ AAGVDSVLIA DVPVEESAPF SKAAKAHGIA
160 170 180 190 200
PIFIAPPNAD ADTLKMVSEQ GEGYTYLLSR AGVTGTESKA GEPIENILTQ
210 220 230 240 250
LAEFNAPPPL LGFGIAEPEQ VRAAIKAGAA GAISGSAVVK IIEAHQHDEA
260
TLLAKLAEFT TAMKAAT
Length:267
Mass (Da):27,806
Last modified:March 21, 2012 - v1
Checksum:iFC55FDE6C55A3E40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB690266 Genomic DNA. Translation: BAL45195.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB690266 Genomic DNA. Translation: BAL45195.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VNDX-ray2.60A/B/C/D/E/F/G/H1-267[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha.
InterProiIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamiPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Ishdia M., Mita M.
    Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: K14-2Imported.
  2. "The crystal strucutre of the tryptophan synthase alpha subunit from the psychrophile Shewanella frigidimarina."
    Mitsuya D., Tanaka S., Matsumura H., Urano N., Takano K., Ogasahara K., Yutani K., Ishida M.
    Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: K14-2Imported.
  3. "Strategy for cold adaptation of the tryptophan synthase alpha subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties."
    Mitsuya D., Tanaka S., Matsumura H., Urano N., Takano K., Ogasahara K., Takehira M., Yutani K., Ishida M.
    J. Biochem. 155:73-82(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).

Entry informationi

Entry nameiH1AFK5_SHEFR
AccessioniPrimary (citable) accession number: H1AFK5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: April 1, 2015
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.