Tryptophan synthase alpha chain - trpA - Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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P00929 (TRPA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·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:	STM1727

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

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-Rule MF_00131
Catalytic activity	L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H₂O. HAMAP-Rule MF_00131
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule 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 Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular_function	protein binding Inferred from physical interaction Ref.9 PubMed 10600108 Ref.10 PubMed 11756454 PubMed 11756456 Ref.11 PubMed 23582331. Source: IntAct tryptophan synthase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpB	P0A2K1	22	EBI-1028423,EBI-1028431

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 268

268

Tryptophan synthase alpha chain HAMAP-Rule MF_00131

PRO_0000098839

Sites

Active site

Proton acceptor

Active site

Proton acceptor

Secondary structure

268

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00929 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F409BF1A931581B5
Show »

FASTA

268

28,671

        10         20         30         40         50         60 
MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL GVPFSDPLAD 

        70         80         90        100        110        120 
GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL MYANLVFNNG IDAFYARCEQ 

       130        140        150        160        170        180 
VGVDSVLVAD VPVEESAPFR QAALRHNIAP IFICPPNADD DLLRQVASYG RGYTYLLSRS 

       190        200        210        220        230        240 
GVTGAENRGA LPLHHLIEKL KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI 

       250        260 
IEKNLASPKQ MLAELRSFVS AMKAASRA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides." Schneider W.P., Nichols B.P., Yanofsky C. Proc. Natl. Acad. Sci. U.S.A. 78:2169-2173(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[4]	"Amino acid sequence studies with the tryptophan synthetase alpha chain of Salmonella typhimurium." Li S.-L., Yanofsky C. J. Biol. Chem. 248:1830-1836(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[5]	"Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium." Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R. J. Biol. Chem. 263:17857-17871(1988) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]	"Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes." Rhee S., Parris K.D., Hyde C.C., Ahmed S.A., Miles E.W., Davies D.R. Biochemistry 36:7664-7680(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]	"Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49." Rhee S., Miles E.W., Davies D.R. J. Biol. Chem. 273:8553-8555(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]	"Refined structure of the native form of the tryptophan synthase multienzyme complex from Salmonella typhimurium." Hyde C.C., Parris K.D., Bhat T.N., Brown C., Ahmed S.A., Miles E.W., Davies D.R. Submitted (JUL-1998) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[9]	"Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase." Sachpatzidis A., Dealwis C., Lubetsky J.B., Liang P.-H., Anderson K.S., Lolis E. Biochemistry 38:12665-12674(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]	"Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase." Weyand M., Schlichting I. J. Biol. Chem. 275:41058-41063(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[11]	"On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase." Kulik V., Weyand M., Seidel R., Niks D., Arac D., Dunn M.F., Schlichting I. J. Mol. Biol. 324:677-690(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-268.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01376 Genomic DNA. Translation: CAA24666.1.
J01810 Genomic DNA. Translation: AAA27235.1.
AE006468 Genomic DNA. Translation: AAL20645.1.

PIR

TSEBAT. A93837.

RefSeq

NP_460686.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A50	X-ray	2.30	A	1-268	[»]
1A5A	X-ray	1.90	A	1-268	[»]
1A5B	X-ray	2.00	A	1-268	[»]
1A5S	X-ray	2.30	A	1-268	[»]
1BEU	X-ray	1.90	A	1-268	[»]
1BKS	X-ray	2.20	A	1-268	[»]
1C29	X-ray	2.30	A	1-268	[»]
1C8V	X-ray	2.20	A	1-268	[»]
1C9D	X-ray	2.30	A	1-268	[»]
1CW2	X-ray	2.00	A	1-268	[»]
1CX9	X-ray	2.30	A	1-268	[»]
1FUY	X-ray	2.25	A	1-268	[»]
1K3U	X-ray	1.70	A	1-268	[»]
1K7E	X-ray	2.30	A	1-268	[»]
1K7F	X-ray	1.90	A	1-268	[»]
1K7X	X-ray	1.70	A	1-268	[»]
1K8X	X-ray	1.90	A	1-268	[»]
1K8Y	X-ray	1.50	A	1-268	[»]
1K8Z	X-ray	1.70	A	1-268	[»]
1KFB	X-ray	1.90	A	1-268	[»]
1KFC	X-ray	1.50	A	1-268	[»]
1KFE	X-ray	1.75	A	1-268	[»]
1KFJ	X-ray	1.80	A	1-268	[»]
1KFK	X-ray	2.40	A	1-268	[»]
1QOP	X-ray	1.40	A	1-268	[»]
1QOQ	X-ray	1.80	A	1-268	[»]
1TJP	X-ray	1.50	A	1-268	[»]
1TTP	X-ray	2.30	A	1-268	[»]
1TTQ	X-ray	2.00	A	1-268	[»]
1UBS	X-ray	1.90	A	1-268	[»]
1WBJ	X-ray	1.50	A	1-268	[»]
2CLE	X-ray	1.50	A	1-268	[»]
2CLF	X-ray	1.70	A	1-268	[»]
2CLH	X-ray	1.70	A	1-268	[»]
2CLI	X-ray	1.70	A	1-268	[»]
2CLK	X-ray	1.50	A	1-268	[»]
2CLL	X-ray	1.60	A	1-268	[»]
2CLM	X-ray	1.51	A	1-268	[»]
2CLO	X-ray	1.50	A	1-268	[»]
2J9X	X-ray	1.90	A	1-268	[»]
2J9Y	X-ray	1.80	A	1-268	[»]
2J9Z	X-ray	1.80	A	1-268	[»]
2RH9	X-ray	1.70	A	1-268	[»]
2RHG	X-ray	2.00	A	1-268	[»]
2TRS	X-ray	2.04	A	1-268	[»]
2TSY	X-ray	2.50	A	1-268	[»]
2TYS	X-ray	1.90	A	1-268	[»]
2WSY	X-ray	3.05	A	1-268	[»]
3CEP	X-ray	2.10	A	1-268	[»]
3PR2	X-ray	1.85	A	2-267	[»]
4HN4	X-ray	1.64	A	1-268	[»]
4HPJ	X-ray	1.45	A	1-268	[»]
4HPX	X-ray	1.65	A	1-268	[»]
4HT3	X-ray	1.30	A	1-268	[»]
4KKX	X-ray	1.77	A	1-268	[»]

ProteinModelPortal

P00929.

SMR

P00929. Positions 1-268.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

DIP

DIP-1033N.

IntAct

P00929. 1 interaction.

MINT

MINT-112862.

STRING

99287.STM1727.

Proteomic databases

PRIDE

P00929.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20645; AAL20645; STM1727.

GeneID

1253246.

KEGG

stm:STM1727.

PATRIC

32381967. VBISalEnt20916_1823.

Phylogenomic databases

HOGENOM

HOG000223814.

K01695.

OMA

NSEGYTY.

OrthoDB

EOG6RVG0K.

PhylomeDB

P00929.

Enzyme and pathway databases

BioCyc

SENT99287:GCTI-1736-MONOMER.

UniPathway

UPA00035; UER00044.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00131. Trp_synth_alpha.

InterPro

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

Pfam

PF00290. Trp_syntA. 1 hit.
[Graphical view]

SUPFAM

SSF51366. SSF51366. 1 hit.

TIGRFAMs

TIGR00262. trpA. 1 hit.

PROSITE

PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00929.

PRO

P00929.

Entry information

Entry name

TRPA_SALTY

Accession

Primary (citable) accession number: P00929

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	July 9, 2014
This is version 142 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents