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H1AFK5 (H1AFK5_SHEFR) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate By similarity. SAAS SAAS018204 HAMAP-Rule MF_00131

Catalytic activity

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O. SAAS SAAS018204 HAMAP-Rule MF_00131

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00131 SAAS SAAS018204

Subunit structure

Tetramer of two alpha and two beta chains By similarity. HAMAP-Rule MF_00131 SAAS SAAS018204

Sequence similarities

Belongs to the TrpA family. HAMAP-Rule MF_00131 RuleBase RU003662

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region93 – 953Sulfate 1 binding PDB 3VND

Sites

Active site501Proton acceptor By similarity HAMAP-Rule MF_00131
Active site611Proton acceptor By similarity HAMAP-Rule MF_00131
Binding site2141Sulfate 2; via amide nitrogen PDB 3VND
Binding site2361Sulfate 2 PDB 3VND

Sequences

Sequence LengthMass (Da)Tools
H1AFK5 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: FC55FDE6C55A3E40

FASTA26727,806
        10         20         30         40         50         60 
MSNRYQAKFA ALKAQDKGAF VPFVTIGDPS PELSLKIIQT LVDNGADALE LGFPFSDPLA 

        70         80         90        100        110        120 
DGPVIQGANL RSLAAGTTSS DCFDIITKVR AQHPDMPIGL LLYANLVFAN GIDEFYTKAQ 

       130        140        150        160        170        180 
AAGVDSVLIA DVPVEESAPF SKAAKAHGIA PIFIAPPNAD ADTLKMVSEQ GEGYTYLLSR 

       190        200        210        220        230        240 
AGVTGTESKA GEPIENILTQ LAEFNAPPPL LGFGIAEPEQ VRAAIKAGAA GAISGSAVVK 

       250        260 
IIEAHQHDEA TLLAKLAEFT TAMKAAT 

« Hide

References

[1]Ishdia M., Mita M.
Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: K14-2 EMBL BAL45195.1.
[2]"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.
Submitted (JAN-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH SULFATE.
[3]"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: K14-2 EMBL BAL45195.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB690266 Genomic DNA. Translation: BAL45195.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VNDX-ray2.60A/B/C/D/E/F/G/H1-267[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00035; UER00044.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00131. Trp_synth_alpha.
InterProIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00262. trpA. 1 hit.
PROSITEPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH1AFK5_SHEFR
AccessionPrimary (citable) accession number: H1AFK5
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: June 11, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)