P0A879 (TRPB_ECOLI) 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:	b1261, JW1253

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay PubMed 4887511. Source: EcoliWiki
Molecular_function	pyridoxal phosphate binding Inferred from direct assay PubMed 350880. Source: EcoliWiki tryptophan synthase activity Inferred from direct assay PubMed 2021608. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 397

396

Tryptophan synthase beta chain HAMAP-Rule MF_00133

PRO_0000098948

Sites

Active site

62

1

Nucleophile Ref.7

Active site

86

1

Proton donor Probable

Amino acid modifications

Modified residue

87

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant

281

1

G → R in mutant TRPB8.

Experimental info

Sequence conflict

78

1

E → K AA sequence Ref.7

Sequence conflict

365

1

N → Z AA sequence Ref.10

Sequence conflict

368 – 369

2

KE → BK AA sequence Ref.10

Secondary structure

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397

Helix Strand Turn

Details...

Helix

19 – 21

3

Helix

22 – 37

16

Helix

39 – 51

13

Beta strand

59 – 61

3

Helix

63 – 66

4

Beta strand

69 – 77

9

Helix

78 – 80

3

Helix

87 – 100

14

Beta strand

105 – 109

5

Beta strand

111 – 113

3

Helix

114 – 125

12

Beta strand

129 – 135

7

Helix

136 – 141

6

Helix

143 – 151

9

Beta strand

155 – 159

5

Helix

166 – 180

15

Turn

181 – 183

3

Beta strand

184 – 186

3

Beta strand

189 – 191

3

Helix

197 – 205

9

Helix

207 – 220

14

Beta strand

225 – 230

6

Beta strand

232 – 234

3

Helix

235 – 241

7

Helix

242 – 244

3

Beta strand

245 – 247

3

Beta strand

250 – 259

10

Turn

262 – 264

3

Helix

270 – 273

4

Beta strand

274 – 279

6

Beta strand

282 – 286

5

Helix

311 – 318

8

Beta strand

321 – 328

8

Helix

329 – 343

15

Helix

349 – 363

15

Beta strand

370 – 376

7

Beta strand

378 – 380

3

Helix

381 – 383

3

Helix

384 – 393

10

Sequences

	Sequence		Length	Mass (Da)
	P0A879 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 16CF49FBD738F06F	FASTA	397	42,983
	10 20 30 40 50 60 MTTLLNPYFG EFGGMYVPQI LMPALRQLEE AFVSAQKDPE FQAQFNDLLK NYAGRPTALT 70 80 90 100 110 120 KCQNITAGTN TTLYLKREDL LHGGAHKTNQ VLGQALLAKR MGKTEIIAET GAGQHGVASA 130 140 150 160 170 180 LASALLGLKC RIYMGAKDVE RQSPNVFRMR LMGAEVIPVH SGSATLKDAC NEALRDWSGS 190 200 210 220 230 240 YETAHYMLGT AAGPHPYPTI VREFQRMIGE ETKAQILERE GRLPDAVIAC VGGGSNAIGM 250 260 270 280 290 300 FADFINETNV GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTE DGQIEESYSI 310 320 330 340 350 360 SAGLDFPSVG PQHAYLNSTG RADYVSITDD EALEAFKTLC LHEGIIPALE SSHALAHALK 370 380 390 MMRENPDKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Milkman R., Bridges M.M. Genetics 133:455-468(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"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] OF 1-394.
[7]	"Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli." Higgins W., Miles E.W., Fairwell T. J. Biol. Chem. 255:512-517(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-100, ACTIVE SITES.
[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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"Tryptophan synthetase beta 2 subunit. Primary structure of the pyridoxyl peptide from the Escherichia coli enzyme." Fluri R., Jackson L.E., Lee W.E., Crawford I.P. J. Biol. Chem. 246:6620-6624(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 77-99.
[10]	"Tryptophan synthetase beta 2 subunit. Application of genetic analysis to the study of primary structure." Cotton R.G.H., Crawford I.P. J. Biol. Chem. 247:1883-1891(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 363-397.
[11]	"Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive 'hinge' region diminishes substrate binding and alters solubility." Zhao G.-P., Somerville R.L. J. Biol. Chem. 267:526-541(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTANT TRPB8.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00365 Genomic DNA. Translation: CAA23663.1.
V00372 Genomic DNA. Translation: CAA23674.1.
U00096 Genomic DNA. Translation: AAC74343.1.
AP009048 Genomic DNA. Translation: BAA14793.1.
J01714 Genomic DNA. Translation: AAA57300.1.
U23489 Genomic DNA. Translation: AAB60034.1.
U23490 Genomic DNA. Translation: AAA65139.1.
U23492 Genomic DNA. Translation: AAA65151.1.
U23493 Genomic DNA. Translation: AAA65157.1.
U23500 Genomic DNA. Translation: AAA65175.1.
U25417 Genomic DNA. Translation: AAA73790.1.
U25418 Genomic DNA. Translation: AAA73796.1.
U25419 Genomic DNA. Translation: AAA73802.1.
U25422 Genomic DNA. Translation: AAA73820.1.
U25423 Genomic DNA. Translation: AAA73826.1.
U25426 Genomic DNA. Translation: AAA73838.1.
U25427 Genomic DNA. Translation: AAA73844.1.
U25428 Genomic DNA. Translation: AAA73850.1.
U25429 Genomic DNA. Translation: AAA73856.1.

PIR

TSECB. H64873.

RefSeq

NP_415777.1. NC_000913.2.
YP_489529.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DH5	X-ray	2.90	A	1-397	[»]
2DH6	X-ray	3.00	A	1-397	[»]

ProteinModelPortal

P0A879.

SMR

P0A879. Positions 3-397.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A879. 6 interactions.

STRING

511145.b1261.

2D gel databases

SWISS-2DPAGE

P0A879.

Proteomic databases

PaxDb

P0A879.

PRIDE

P0A879.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74343; AAC74343; b1261.
BAA14793; BAA14793; BAA14793.

GeneID

12930549.
945768.

KEGG

ecj:Y75_p1235.
eco:b1261.

PATRIC

32117782. VBIEscCol129921_1311.

Organism-specific databases

EchoBASE

EB1018.

EcoGene

EG11025. trpB.

Phylogenomic databases

eggNOG

COG0133.

HOGENOM

HOG000161710.

KO

K01696.

OMA

WVANVDS.

ProtClustDB

PRK04346.

Enzyme and pathway databases

BioCyc

EcoCyc:TRYPSYN-BPROTEIN.
ECOL316407:JW1253-MONOMER.
MetaCyc:TRYPSYN-BPROTEIN.

SABIO-RK

P0A879.

UniPathway

UPA00035; UER00044.

Gene expression databases

Genevestigator

P0A879.

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

P0A879.

Entry information

Entry name

TRPB_ECOLI

Accession

Primary (citable) accession number: P0A879
Secondary accession number(s): P00932, P78146

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program