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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 (NADP(+)) (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 (NADP(+)) (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)DescriptionActionsGraphical viewLength
Binding sitei101Pyridoxal phosphate1 Publication1
Binding sitei209Pyridoxal phosphate1 Publication1
Binding sitei314Pyridoxal phosphate1 Publication1

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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003961091 – 368Branched-chain-amino-acid aminotransferaseAdd BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei204N6-(pyridoxal phosphate)lysine1
Cross-linki299Isoglutamyl 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

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 27Combined sources9
Beta strandi31 – 33Combined sources3
Beta strandi37 – 45Combined sources9
Turni46 – 48Combined sources3
Beta strandi49 – 58Combined sources10
Beta strandi61 – 63Combined sources3
Helixi69 – 72Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi80 – 84Combined sources5
Beta strandi90 – 94Combined sources5
Helixi95 – 108Combined sources14
Helixi116 – 130Combined sources15
Helixi131 – 133Combined sources3
Beta strandi137 – 140Combined sources4
Beta strandi142 – 151Combined sources10
Beta strandi162 – 174Combined sources13
Beta strandi176 – 178Combined sources3
Beta strandi180 – 182Combined sources3
Beta strandi184 – 188Combined sources5
Helixi206 – 221Combined sources16
Beta strandi225 – 230Combined sources6
Turni232 – 234Combined sources3
Beta strandi237 – 241Combined sources5
Beta strandi244 – 251Combined sources8
Helixi253 – 255Combined sources3
Beta strandi257 – 260Combined sources4
Beta strandi265 – 267Combined sources3
Helixi271 – 283Combined sources13
Beta strandi286 – 289Combined sources4
Helixi294 – 303Combined sources10
Beta strandi305 – 313Combined sources9
Turni314 – 316Combined sources3
Beta strandi317 – 326Combined sources10
Beta strandi329 – 332Combined sources4
Helixi340 – 353Combined sources14
Beta strandi364 – 366Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DTFX-ray2.20A/B2-368[»]
3DTGX-ray1.90A/B2-368[»]
3JZ6X-ray1.90A/B2-368[»]
ProteinModelPortaliA0R066.
SMRiA0R066.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0R066.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni271 – 272Pyridoxal phosphate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CM2. Bacteria.
COG0115. LUCA.
HOGENOMiHOG000276704.
KOiK00826.
OMAiNFFGITH.
OrthoDBiPOG091H02MO.

Family and domain databases

CDDicd01557. BCAT_beta_family. 1 hit.
InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
IPR033939. BCAT_family.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DTFX-ray2.20A/B2-368[»]
3DTGX-ray1.90A/B2-368[»]
3JZ6X-ray1.90A/B2-368[»]
ProteinModelPortaliA0R066.
SMRiA0R066.
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.
OrthoDBiPOG091H02MO.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
BRENDAi2.6.1.42. 3512.

Miscellaneous databases

EvolutionaryTraceiA0R066.

Family and domain databases

CDDicd01557. BCAT_beta_family. 1 hit.
InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
IPR033939. BCAT_family.
[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...

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 30, 2016
This is version 67 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.