Tryptophan synthase alpha chain - Escherichia coli (strain K12)

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P0A877 (TRPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tryptophan synthase alpha chain
EC=4.2.1.20

Gene names

Name:	trpA
Ordered Locus Names:	b1260, JW1252

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP MF_00131
Catalytic activity	L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H₂O. HAMAP MF_00131
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP MF_00131
Subunit structure	Tetramer of two alpha and two beta chains.
Sequence similarities	Belongs to the TrpA family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: EcoliWiki
Molecular function	sulfate binding Inferred from physical interaction. Source: EcoliWiki tryptophan synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 268

268

Tryptophan synthase alpha chain HAMAP MF_00131

PRO_0000098778

Sites

Active site

Proton acceptor By similarity

Active site

Proton acceptor By similarity

Natural variations

Natural variant

209 – 224

LQGFG…VKAAI → IAGFWYFRPGSGKSSD in mutant TrpA46-Asp-PR3.

Secondary structure

268

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A877 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 028223DB2B666CC6
Show »

FASTA

268

28,724

        10         20         30         40         50         60 
MERYESLFAQ LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADALEL GIPFSDPLAD 

        70         80         90        100        110        120 
GPTIQNATLR AFAAGVTPAQ CFEMLALIRQ KHPTIPIGLL MYANLVFNKG IDEFYAQCEK 

       130        140        150        160        170        180 
VGVDSVLVAD VPVEESAPFR QAALRHNVAP IFICPPNADD DLLRQIASYG RGYTYLLSRA 

       190        200        210        220        230        240 
GVTGAENRAA LPLNHLVAKL KEYNAAPPLQ GFGISAPDQV KAAIDAGAAG AISGSAIVKI 

       250        260 
IEQHINEPEK MLAALKVFVQ PMKAATRS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The amino acid sequence of the A protein (alpha subunit) of the tryptophan synthetase of Escherichia coli." Guest J.R., Drapeau G.R., Carlton B.C., Yanofsky C. J. Biol. Chem. 242:5442-5446(1967) [PubMed: 4863752] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison." Nichols B.P., Yanofsky C. Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979) [PubMed: 388433] [Abstract] Cited for: PROTEIN SEQUENCE.
[3]	"The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M. Nucleic Acids Res. 9:6647-6668(1981) [PubMed: 7038627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Milkman R., Bridges M.M. Genetics 133:455-468(1993) [PubMed: 8095913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[9]	"Missense and nonsense suppressors can correct frameshift mutations." Tucker S.D., Murgola E.J., Pagel F.T. Biochimie 71:729-739(1989) [PubMed: 2502189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-225 (MUTANT TRPA46-ASP-PR3). Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00364 Genomic DNA. Translation: CAA23662.1.
V00372 Genomic DNA. Translation: CAA23675.1.
J01714 Genomic DNA. Translation: AAA57301.1.
U23489 Genomic DNA. Translation: AAB60035.1.
U23490 Genomic DNA. Translation: AAA65140.1.
U23491 Genomic DNA. Translation: AAA65146.1.
U23492 Genomic DNA. Translation: AAA65152.1.
U23494 Genomic DNA. Translation: AAA65164.1.
U25417 Genomic DNA. Translation: AAA73791.1.
U25418 Genomic DNA. Translation: AAA73797.1.
U25419 Genomic DNA. Translation: AAA73803.1.
U25420 Genomic DNA. Translation: AAA73809.1.
U25421 Genomic DNA. Translation: AAA73815.1.
U25422 Genomic DNA. Translation: AAA73821.1.
U00096 Genomic DNA. Translation: AAC74342.1.
AP009048 Genomic DNA. Translation: BAA14792.1.
X16698 Genomic DNA. Translation: CAA34671.1.

PIR

TSECA. E93746.

RefSeq

NP_415776.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V7Y	X-ray	2.50	A/B	1-268	[»]
1WQ5	X-ray	2.30	A/B	1-268	[»]
1XC4	X-ray	2.80	A/B	1-268	[»]
1XCF	X-ray	1.80	A/B	1-268	[»]

ProteinModelPortal

P0A877.

SMR

P0A877. Positions 1-268.

DisProt

DP00252.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35957N.

IntAct

P0A877. 5 interactions.

2D gel databases

SWISS-2DPAGE

P0A877.

2DBase-Ecoli

P0A877.

ECO2DBASE

E025.5. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004452; EBESCP00000004452; EBESCG00000003632.
EBESCT00000004453; EBESCP00000004453; EBESCG00000003632.
EBESCT00000014719; EBESCP00000014010; EBESCG00000013780.

GeneID

946204.

GenomeReviews

Gene locus JW1252 in contig AP009048_GR.
Gene locus b1260 in contig U00096_GR.

KEGG

ecj:JW1252.
eco:b1260.

PATRIC

32117780. VBIEscCol129921_1310.

Organism-specific databases

EchoBASE

EB1017.

EcoGene

EG11024. trpA.

Phylogenomic databases

eggNOG

COG0159.

GeneTree

EBGT00050000009400.

HOGENOM

HBG391690.

OMA

NPIYIYG.

PhylomeDB

P0A877.

ProtClustDB

PRK13111.

Enzyme and pathway databases

BioCyc

EcoCyc:TRYPSYN-APROTEIN.
MetaCyc:TRYPSYN-APROTEIN.

Gene expression databases

Genevestigator

P0A877.

Family and domain databases

HAMAP

MF_00131. Trp_synth_alpha.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

K01695.

Pfam

PF00290. Trp_syntA. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 1 hit.

TIGRFAMs

TIGR00262. TrpA. 1 hit.

PROSITE

PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRPA_ECOLI

Accession

Primary (citable) accession number: P0A877
Secondary accession number(s): P00928, Q47669

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents