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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: -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), Acetolactate synthase (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), 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-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase large subunit (leuC), 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-isopropylmalate dehydratase small subunit (leuD)
  3. 3-isopropylmalate dehydrogenase (leuB), 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), Acetolactate synthase (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD), 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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMSME246196:G1H7P-4263-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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium fortuitum complex
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
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.

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
PATRICifig|246196.19.peg.4197

Similar proteinsi

Entry informationi

Entry nameiILVE_MYCS2
AccessioniPrimary (citable) accession number: A0R066
Secondary accession number(s): I7FPI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: May 23, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health