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Protein

Branched-chain-amino-acid aminotransferase

Gene

ilvE

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Unreviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.UniRule annotation
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.UniRule annotation
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine 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-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-leucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC)
  3. 3-isopropylmalate dehydrogenase (leuB)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-leucine 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-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine 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-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminotransferaseUniRule annotationImported, Transferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation
LigandPyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciSMUT210007:G1FZX-1142-MONOMER
BRENDAi2.6.1.42 5941
UniPathwayiUPA00047; UER00058
UPA00048; UER00073
UPA00049; UER00062

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferaseUniRule annotation (EC:2.6.1.42UniRule annotation)
Gene namesi
Name:ilvEImported
Ordered Locus Names:SMU_1203Imported
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)Imported
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei184N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_1203

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DQNX-ray1.97A2-341[»]
ProteinModelPortaliQ8DTW7
SMRiQ8DTW7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CM2 Bacteria
COG0115 LUCA
KOiK00826
OMAiNFFGITH
PhylomeDBiQ8DTW7

Family and domain databases

CDDicd01557 BCAT_beta_family, 1 hit
InterProiView protein in InterPro
IPR001544 Aminotrans_IV
IPR018300 Aminotrans_IV_CS
IPR036038 Aminotransferase-like
IPR005786 B_amino_transII
IPR033939 BCAT_family
PfamiView protein in Pfam
PF01063 Aminotran_4, 1 hit
PIRSFiPIRSF006468 BCAT1, 1 hit
SUPFAMiSSF56752 SSF56752, 1 hit
TIGRFAMsiTIGR01123 ilvE_II, 1 hit
PROSITEiView protein in PROSITE
PS00770 AA_TRANSFER_CLASS_4, 1 hit

Sequencei

Sequence statusi: Complete.

Q8DTW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVDLDWKNL GFEYHKLPFR YISYYKDGKW DDGKLTEDAT LHISESSPAL
60 70 80 90 100
HYGQEAFEGL KAYRTKDGSV QLFRPNMNAE RLQRTADRLL MPQVPTDKFI
110 120 130 140 150
DAAKQVVRAN EEYVPPYGTG ATLYLRPLLI GVGDVIGVHP ADEYIFTIFA
160 170 180 190 200
MPVGNYFKGG LAPTNFLIQD DYDRAAPHGT GAAKVGGNYA ASLLPGKVAH
210 220 230 240 250
ERQFSDVIYL DPATHTKIEE VGSANFFGIT KDNEFITPLS PSILPSVTKY
260 270 280 290 300
SLLYLAEHRF GMKAIEGDVC VDELDKFVEA GACGTAAVIS PIGGVQHGDD
310 320 330 340
FHVFYSETEV GPVTHKLYDE LTGIQFGDVK APEGWIYKVD D
Length:341
Mass (Da):37,732
Last modified:March 1, 2003 - v1
Checksum:iEF5AAD29AEF56125
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA Translation: AAN58889.1
RefSeqiNP_721583.1, NC_004350.2
WP_002263260.1, NC_004350.2

Genome annotation databases

EnsemblBacteriaiAAN58889; AAN58889; SMU_1203
GeneIDi1029342
KEGGismu:SMU_1203
PATRICifig|210007.7.peg.1077

Similar proteinsi

Entry informationi

Entry nameiQ8DTW7_STRMU
AccessioniPrimary (citable) accession number: Q8DTW7
Entry historyiIntegrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: February 28, 2018
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported