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Protein

Branched-chain-amino-acid aminotransferase

Gene

ilvE

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.1 Publication

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Inbibited by ammonium sulfate at millimolar concentrations and by O-benzylhydroxylamine (Obe).1 Publication

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), 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.
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 large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  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.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (ilvB), Acetolactate synthase small subunit (ilvH)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011Pyridoxal phosphate1 Publication
Binding sitei209 – 2091Pyridoxal phosphate1 Publication
Binding sitei314 – 3141Pyridoxal phosphate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-4276-MONOMER.
BRENDAi2.6.1.42. 3512.
UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase (EC:2.6.1.42)
Short name:
BCAT
Gene namesi
Name:ilvE
Ordered Locus Names:MSMEG_4276, MSMEI_4176
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Branched-chain-amino-acid aminotransferasePRO_0000396109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-(pyridoxal phosphate)lysine
Cross-linki299 – 299Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi246196.MSMEG_4276.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 279Combined sources
Beta strandi31 – 333Combined sources
Beta strandi37 – 459Combined sources
Turni46 – 483Combined sources
Beta strandi49 – 5810Combined sources
Beta strandi61 – 633Combined sources
Helixi69 – 724Combined sources
Beta strandi75 – 773Combined sources
Beta strandi80 – 845Combined sources
Beta strandi90 – 945Combined sources
Helixi95 – 10814Combined sources
Helixi116 – 13015Combined sources
Helixi131 – 1333Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi142 – 15110Combined sources
Beta strandi162 – 17413Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1885Combined sources
Helixi206 – 22116Combined sources
Beta strandi225 – 2306Combined sources
Turni232 – 2343Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 2518Combined sources
Helixi253 – 2553Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi265 – 2673Combined sources
Helixi271 – 28313Combined sources
Beta strandi286 – 2894Combined sources
Helixi294 – 30310Combined sources
Beta strandi305 – 3139Combined sources
Turni314 – 3163Combined sources
Beta strandi317 – 32610Combined sources
Beta strandi329 – 3324Combined sources
Helixi340 – 35314Combined sources
Beta strandi364 – 3663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DTFX-ray2.20A/B2-368[»]
3DTGX-ray1.90A/B2-368[»]
3JZ6X-ray1.90A/B2-368[»]
ProteinModelPortaliA0R066.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0R066.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 2722Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CM2. Bacteria.
COG0115. LUCA.
HOGENOMiHOG000276704.
KOiK00826.
OMAiNFFGITH.
OrthoDBiEOG67MF3R.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0R066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSGPLEFTV SANTNPATDA VRESILANPG FGKYYTDHMV SIDYTVDEGW
60 70 80 90 100
HNAQVIPYGP IQLDPSAIVL HYGQEIFEGL KAYRWADGSI VSFRPEANAA
110 120 130 140 150
RLQSSARRLA IPELPEEVFI ESLRQLIAVD EKWVPPAGGE ESLYLRPFVI
160 170 180 190 200
ATEPGLGVRP SNEYRYLLIA SPAGAYFKGG IKPVSVWLSH EYVRASPGGT
210 220 230 240 250
GAAKFGGNYA ASLLAQAQAA EMGCDQVVWL DAIERRYVEE MGGMNLFFVF
260 270 280 290 300
GSGGSARLVT PELSGSLLPG ITRDSLLQLA TDAGFAVEER KIDVDEWQKK
310 320 330 340 350
AGAGEITEVF ACGTAAVITP VSHVKHHDGE FTIADGQPGE ITMALRDTLT
360
GIQRGTFADT HGWMARLN
Length:368
Mass (Da):39,837
Last modified:January 9, 2007 - v1
Checksum:i19C86C028296591D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74679.1.
CP001663 Genomic DNA. Translation: AFP40633.1.
RefSeqiWP_011729696.1. NZ_CP009494.1.
YP_888554.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74679; ABK74679; MSMEG_4276.
AFP40633; AFP40633; MSMEI_4176.
GeneIDi4532447.
KEGGimsb:LJ00_21200.
msg:MSMEI_4176.
msm:MSMEG_4276.
PATRICi18080911. VBIMycSme59918_4197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74679.1.
CP001663 Genomic DNA. Translation: AFP40633.1.
RefSeqiWP_011729696.1. NZ_CP009494.1.
YP_888554.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DTFX-ray2.20A/B2-368[»]
3DTGX-ray1.90A/B2-368[»]
3JZ6X-ray1.90A/B2-368[»]
ProteinModelPortaliA0R066.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_4276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74679; ABK74679; MSMEG_4276.
AFP40633; AFP40633; MSMEI_4176.
GeneIDi4532447.
KEGGimsb:LJ00_21200.
msg:MSMEI_4176.
msm:MSMEG_4276.
PATRICi18080911. VBIMycSme59918_4197.

Phylogenomic databases

eggNOGiENOG4105CM2. Bacteria.
COG0115. LUCA.
HOGENOMiHOG000276704.
KOiK00826.
OMAiNFFGITH.
OrthoDBiEOG67MF3R.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
BioCyciMSME246196:GJ4Y-4276-MONOMER.
BRENDAi2.6.1.42. 3512.

Miscellaneous databases

EvolutionaryTraceiA0R066.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: PUPYLATION AT LYS-299, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design."
    Castell A., Mille C., Unge T.
    Acta Crystallogr. D 66:549-557(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, FUNCTION AS AN AMINOTRANSFERASE, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiILVE_MYCS2
AccessioniPrimary (citable) accession number: A0R066
Secondary accession number(s): I7FPI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: November 11, 2015
This is version 64 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.