P0A2K1 (TRPB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan synthase beta chain
EC=4.2.1.20

Gene names

Name:	trpB
Ordered Locus Names:	STM1726

Organism

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

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. HAMAP-Rule MF_00133
Catalytic activity	L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O. HAMAP-Rule MF_00133
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00133
Subunit structure	Tetramer of two alpha and two beta chains.
Sequence similarities	Belongs to the TrpB family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	tryptophan synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trpA	P00929	20	EBI-1028431,EBI-1028423

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP-Rule MF_00133

Chain

2 – 397

396

Tryptophan synthase beta chain HAMAP-Rule MF_00133

PRO_0000098994

Amino acid modifications

Modified residue

87

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00133

Experimental info

Sequence conflict

34

1

S → R in CAA24667. Ref.1

Sequence conflict

34

1

S → R in AAA27234. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

397

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

12 – 17

6

Helix

19 – 21

3

Helix

22 – 36

15

Helix

39 – 51

13

Turn

52 – 54

3

Beta strand

59 – 61

3

Helix

63 – 66

4

Beta strand

69 – 77

9

Helix

78 – 80

3

Helix

88 – 100

13

Beta strand

105 – 113

9

Helix

114 – 126

13

Beta strand

129 – 135

7

Helix

136 – 141

6

Helix

143 – 151

9

Beta strand

155 – 159

5

Beta strand

161 – 163

3

Helix

166 – 180

15

Turn

181 – 183

3

Beta strand

184 – 186

3

Beta strand

189 – 191

3

Helix

197 – 203

7

Turn

204 – 206

3

Helix

207 – 220

14

Beta strand

225 – 230

6

Beta strand

232 – 234

3

Helix

235 – 241

7

Helix

242 – 244

3

Beta strand

250 – 259

10

Helix

262 – 264

3

Helix

270 – 273

4

Beta strand

274 – 279

6

Beta strand

281 – 286

6

Beta strand

290 – 292

3

Helix

302 – 304

3

Helix

311 – 318

8

Beta strand

321 – 328

8

Helix

329 – 343

15

Helix

349 – 364

16

Beta strand

370 – 376

7

Beta strand

378 – 380

3

Helix

381 – 383

3

Helix

384 – 390

7

Turn

393 – 395

3

Sequences

	Sequence		Length	Mass (Da)
	P0A2K1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 73D210F5C6F2FEBD	FASTA	397	42,868
	10 20 30 40 50 60 MTTLLNPYFG EFGGMYVPQI LMPALNQLEE AFVSAQKDPE FQAQFADLLK NYAGRPTALT 70 80 90 100 110 120 KCQNITAGTR TTLYLKREDL LHGGAHKTNQ VLGQALLAKR MGKSEIIAET GAGQHGVASA 130 140 150 160 170 180 LASALLGLKC RIYMGAKDVE RQSPNVFRMR LMGAEVIPVH SGSATLKDAC NEALRDWSGS 190 200 210 220 230 240 YETAHYMLGT AAGPHPYPTI VREFQRMIGE ETKAQILDKE GRLPDAVIAC VGGGSNAIGM 250 260 270 280 290 300 FADFINDTSV GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTA DGQIEESYSI 310 320 330 340 350 360 SAGLDFPSVG PQHAYLNSIG RADYVSITDD EALEAFKTLC RHEGIIPALE SSHALAHALK 370 380 390 MMREQPEKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimurium." Crawford I.P., Nichols B.P., Yanofsky C. J. Mol. Biol. 142:489-502(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., 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.
[3]	"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] OF 375-397.
[4]	"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] OF 375-397.
[5]	"Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella typhimurium." Selker E., Yanofsky C. J. Mol. Biol. 130:135-143(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[6]	"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).
[7]	"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) OF WILD TYPE AND TYR-87 MUTANTS IN COMPLEX WITH L-SERINE, PYRIDOXAL PHOSPHATE AT LYS-87.
[8]	"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).
[9]	"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).
[10]	"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).
[11]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01377 Genomic DNA. Translation: CAA24667.1.
J01810 Genomic DNA. Translation: AAA27234.1.
AE006468 Genomic DNA. Translation: AAL20644.1.
V01376 Genomic DNA. Translation: CAA24665.1.
V00364 Genomic DNA. Translation: CAA23661.1.
M24299 Genomic DNA. Translation: AAA99293.1.

PIR

TSEBBT. A01156.

RefSeq

NP_460685.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A50	X-ray	2.30	B	2-396	[»]
1A5A	X-ray	1.90	B	1-395	[»]
1A5B	X-ray	2.00	B	1-395	[»]
1A5S	X-ray	2.30	B	1-397	[»]
1BEU	X-ray	1.90	B	2-395	[»]
1BKS	X-ray	2.20	B	2-396	[»]
1C29	X-ray	2.30	B	1-397	[»]
1C8V	X-ray	2.20	B	1-397	[»]
1C9D	X-ray	2.30	B	1-397	[»]
1CW2	X-ray	2.00	B	1-397	[»]
1CX9	X-ray	2.30	B	1-397	[»]
1FUY	X-ray	2.25	B	2-397	[»]
1K3U	X-ray	1.70	B	2-396	[»]
1K7E	X-ray	2.30	B	2-396	[»]
1K7F	X-ray	1.90	B	2-396	[»]
1K7X	X-ray	1.70	B	2-396	[»]
1K8X	X-ray	1.90	B	1-397	[»]
1K8Y	X-ray	1.50	B	2-396	[»]
1K8Z	X-ray	1.70	B	2-396	[»]
1KFB	X-ray	1.90	B	2-397	[»]
1KFC	X-ray	1.50	B	1-397	[»]
1KFE	X-ray	1.75	B	2-395	[»]
1KFJ	X-ray	1.80	B	1-397	[»]
1KFK	X-ray	2.40	B	1-397	[»]
1QOP	X-ray	1.40	B	2-397	[»]
1QOQ	X-ray	1.80	B	2-396	[»]
1TJP	X-ray	1.50	B	2-397	[»]
1TTP	X-ray	2.30	B	1-397	[»]
1TTQ	X-ray	2.00	B	1-397	[»]
1UBS	X-ray	1.90	B	1-395	[»]
1WBJ	X-ray	1.50	B	2-397	[»]
2CLE	X-ray	1.50	B	2-396	[»]
2CLF	X-ray	1.70	B	2-396	[»]
2CLH	X-ray	1.70	B	2-396	[»]
2CLI	X-ray	1.70	B	2-396	[»]
2CLK	X-ray	1.50	B	2-396	[»]
2CLL	X-ray	1.60	B	2-396	[»]
2CLM	X-ray	1.51	B	2-396	[»]
2CLO	X-ray	1.50	B	2-396	[»]
2J9X	X-ray	1.90	B	2-396	[»]
2J9Y	X-ray	1.80	B	1-397	[»]
2J9Z	X-ray	1.80	B	1-397	[»]
2RH9	X-ray	1.70	B	1-397	[»]
2RHG	X-ray	2.00	B	1-397	[»]
2TRS	X-ray	2.04	B	1-395	[»]
2TSY	X-ray	2.50	B	1-395	[»]
2TYS	X-ray	1.90	B	1-397	[»]
2WSY	X-ray	3.05	B	2-396	[»]
3CEP	X-ray	2.10	B	2-397	[»]
3PR2	X-ray	1.85	B	3-393	[»]

ProteinModelPortal

P0A2K1.

SMR

P0A2K1. Positions 2-395.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35707N.

IntAct

P0A2K1. 1 interaction.

MINT

MINT-112874.

STRING

99287.STM1726.

Proteomic databases

PRIDE

P0A2K1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20644; AAL20644; STM1726.

GeneID

1253245.

KEGG

stm:STM1726.

PATRIC

32381965. VBISalEnt20916_1822.

Phylogenomic databases

HOGENOM

HOG000161710.

KO

K01696.

OMA

REDLCHT.

ProtClustDB

PRK04346.

Enzyme and pathway databases

UniPathway

UPA00035; UER00044.

Family and domain databases

HAMAP

MF_00133. Trp_synth_beta.

InterPro

IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
IPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
[Graphical view]

PANTHER

PTHR10314:SF3. PTHR10314:SF3. 1 hit.

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

PIRSF

PIRSF001413. Trp_syn_beta. 1 hit.

SUPFAM

SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.

TIGRFAMs

TIGR00263. trpB. 1 hit.

PROSITE

PS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A2K1.

Entry information

Entry name

TRPB_SALTY

Accession

Primary (citable) accession number: P0A2K1
Secondary accession number(s): P00933, Q56141

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program