Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tryptophan synthase beta chain

Gene

trpB

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.UniRule annotation

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD)
  3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF), N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
  4. Indole-3-glycerol phosphate synthase (trpC), Indole-3-glycerol phosphate synthase (trpC), Indole-3-glycerol phosphate synthase (trpC)
  5. Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciANTHRA:TRPB-MONOMER.
BANT260799:GJAJ-1236-MONOMER.
BANT261594:GJ7F-1290-MONOMER.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase beta chainUniRule annotation (EC:4.2.1.20UniRule annotation)
Gene namesi
Name:trpBUniRule annotation
Ordered Locus Names:BA_1253, GBAA_1253, BAS1161
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Tryptophan synthase beta chainPRO_0000098914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.UniRule annotation

Protein-protein interaction databases

IntActiQ81TL8. 4 interactions.
STRINGi198094.BA_1253.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3916Combined sources
Helixi42 – 5413Combined sources
Beta strandi62 – 643Combined sources
Helixi66 – 727Combined sources
Beta strandi74 – 818Combined sources
Helixi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 10514Combined sources
Beta strandi109 – 1179Combined sources
Helixi118 – 13013Combined sources
Beta strandi133 – 1397Combined sources
Helixi140 – 1445Combined sources
Helixi147 – 1559Combined sources
Beta strandi159 – 1635Combined sources
Helixi170 – 18415Combined sources
Turni185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi195 – 1984Combined sources
Helixi201 – 22424Combined sources
Beta strandi229 – 2346Combined sources
Helixi242 – 2454Combined sources
Helixi246 – 2483Combined sources
Beta strandi254 – 2618Combined sources
Helixi318 – 3225Combined sources
Beta strandi325 – 3317Combined sources
Helixi333 – 34715Combined sources
Helixi353 – 36513Combined sources
Helixi366 – 3683Combined sources
Beta strandi374 – 3796Combined sources
Helixi383 – 3853Combined sources
Helixi387 – 3937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NEGX-ray2.20A/B1-397[»]
ProteinModelPortaliQ81TL8.
SMRiQ81TL8. Positions 12-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CG0. Bacteria.
COG0133. LUCA.
HOGENOMiHOG000161710.
KOiK01696.
OMAiIPEMLYP.
OrthoDBiEOG6GFGH7.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81TL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYAYPDEKG HYGIYGGRYV PETLMQSVLE LEEAYKEAME DEAFQKELNH
60 70 80 90 100
YLKTYVGRET PLYFAENMTE YCGGAKIYLK REDLNHTGAH KINNTIGQAL
110 120 130 140 150
LAVRMGKKKV VAETGAGQHG VATATVCALL GLECVIFMGE EDVRRQKLNV
160 170 180 190 200
FRMELLGAKV ESVAAGSGTL KDAVNEALRY WVSHVHDTHY IMGSVLGPHP
210 220 230 240 250
FPQIVRDFQS VIGNETKKQY EALEGKLPEA VVACIGGGSN AMGMFYPFVH
260 270 280 290 300
DEEVALYGVE AAGKGVHTEK HAATLTKGSV GVLHGSMMYL LQNEEGQIQE
310 320 330 340 350
AHSISAGLDY PGVGPEHSLL KDIGRVSYHS ITDDEALEAF QLLTKKEGII
360 370 380 390
PALESSHAVA YALKLAPQMK EDEGLVICLS GRGDKDVESI KRYMEEV
Length:397
Mass (Da):43,590
Last modified:June 1, 2003 - v1
Checksum:i0C56E4584F798313
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP25211.1.
AE017334 Genomic DNA. Translation: AAT30343.1.
AE017225 Genomic DNA. Translation: AAT53483.1.
RefSeqiNP_843725.1. NC_003997.3.
WP_001105001.1. NZ_LHUO01000014.1.
YP_027432.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP25211; AAP25211; BA_1253.
AAT30343; AAT30343; GBAA_1253.
AAT53483; AAT53483; BAS1161.
GeneIDi1086833.
2851906.
KEGGiban:BA_1253.
bar:GBAA_1253.
bat:BAS1161.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP25211.1.
AE017334 Genomic DNA. Translation: AAT30343.1.
AE017225 Genomic DNA. Translation: AAT53483.1.
RefSeqiNP_843725.1. NC_003997.3.
WP_001105001.1. NZ_LHUO01000014.1.
YP_027432.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NEGX-ray2.20A/B1-397[»]
ProteinModelPortaliQ81TL8.
SMRiQ81TL8. Positions 12-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81TL8. 4 interactions.
STRINGi198094.BA_1253.

Protocols and materials databases

DNASUi1086833.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP25211; AAP25211; BA_1253.
AAT30343; AAT30343; GBAA_1253.
AAT53483; AAT53483; BAS1161.
GeneIDi1086833.
2851906.
KEGGiban:BA_1253.
bar:GBAA_1253.
bat:BAS1161.

Phylogenomic databases

eggNOGiENOG4105CG0. Bacteria.
COG0133. LUCA.
HOGENOMiHOG000161710.
KOiK01696.
OMAiIPEMLYP.
OrthoDBiEOG6GFGH7.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.
BioCyciANTHRA:TRPB-MONOMER.
BANT260799:GJAJ-1236-MONOMER.
BANT261594:GJ7F-1290-MONOMER.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.

Entry informationi

Entry nameiTRPB_BACAN
AccessioniPrimary (citable) accession number: Q81TL8
Secondary accession number(s): Q6I1U8, Q6KVP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: January 20, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.