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Q8DTW7 (Q8DTW7_STRMU) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Branched-chain-amino-acid aminotransferase RuleBase RU004517

EC=2.6.1.42 RuleBase RU004517
Gene names
Name:ilvE EMBL AAN58889.1
Ordered Locus Names:SMU_1203 EMBL AAN58889.1
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP] EMBL AAN58889.1
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. RuleBase RU004517

L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. RuleBase RU004517

L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate. RuleBase RU004517

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. RuleBase RU004519

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. RuleBase RU004519

Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. RuleBase RU004519

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. RuleBase RU004106

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue1841N6-(pyridoxal phosphate)lysine By similarity PIRSR PIRSR006468-1

Sequences

Sequence LengthMass (Da)Tools
Q8DTW7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EF5AAD29AEF56125

FASTA34137,732
        10         20         30         40         50         60 
MTVDLDWKNL GFEYHKLPFR YISYYKDGKW DDGKLTEDAT LHISESSPAL HYGQEAFEGL 

        70         80         90        100        110        120 
KAYRTKDGSV QLFRPNMNAE RLQRTADRLL MPQVPTDKFI DAAKQVVRAN EEYVPPYGTG 

       130        140        150        160        170        180 
ATLYLRPLLI GVGDVIGVHP ADEYIFTIFA MPVGNYFKGG LAPTNFLIQD DYDRAAPHGT 

       190        200        210        220        230        240 
GAAKVGGNYA ASLLPGKVAH ERQFSDVIYL DPATHTKIEE VGSANFFGIT KDNEFITPLS 

       250        260        270        280        290        300 
PSILPSVTKY SLLYLAEHRF GMKAIEGDVC VDELDKFVEA GACGTAAVIS PIGGVQHGDD 

       310        320        330        340 
FHVFYSETEV GPVTHKLYDE LTGIQFGDVK APEGWIYKVD D 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H., Najar F., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.
[2]"Structure of the branched-chain aminotransferase from Streptococcus mutans."
Ruan J., Hu J., Yin A., Wu W., Cong X., Feng X., Li S.
Acta Crystallogr. D 68:996-1002(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 2-341.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58889.1.
RefSeqNP_721583.1. NC_004350.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DQNX-ray1.97A2-341[»]
ProteinModelPortalQ8DTW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58889; AAN58889; SMU_1203.
GeneID1029342.
KEGGsmu:SMU_1203.
PATRIC19664495. VBIStrMut61772_1077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00826.
OMAFRPTKNA.
OrthoDBEOG67MF3R.
PhylomeDBQ8DTW7.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-1142-MONOMER.
UniPathwayUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Family and domain databases

InterProIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFPIRSF006468. BCAT1. 1 hit.
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR01123. ilvE_II. 1 hit.
PROSITEPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ8DTW7_STRMU
AccessionPrimary (citable) accession number: Q8DTW7
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)