ILVE_MYCS2
ID ILVE_MYCS2 Reviewed; 368 AA.
AC A0R066; I7FPI5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
GN Name=ilvE; OrderedLocusNames=MSMEG_4276, MSMEI_4176;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PUPYLATION AT LYS-299, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP FUNCTION AS AN AMINOTRANSFERASE, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=20445230; DOI=10.1107/s0907444910004877;
RA Castell A., Mille C., Unge T.;
RT "Structural analysis of mycobacterial branched-chain aminotransferase:
RT implications for inhibitor design.";
RL Acta Crystallogr. D 66:549-557(2010).
CC -!- FUNCTION: Catalyzes the reversible transfers of an amino group from
CC glutamate to the alpha-ketoacid of the respective amino acid in the
CC final step in the biosynthesis of branchedchain amino acids. The amino
CC acids can be ranked in the following order with respect to their
CC efficiency as amino donor: Leu > Ile > Val.
CC {ECO:0000269|PubMed:20445230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20445230};
CC -!- ACTIVITY REGULATION: Inbibited by ammonium sulfate at millimolar
CC concentrations and by O-benzylhydroxylamine (Obe).
CC {ECO:0000269|PubMed:20445230}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20445230}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK74679.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40633.1; -; Genomic_DNA.
DR RefSeq; WP_011729696.1; NZ_SIJM01000003.1.
DR RefSeq; YP_888554.1; NC_008596.1.
DR PDB; 3DTF; X-ray; 2.20 A; A/B=2-368.
DR PDB; 3DTG; X-ray; 1.90 A; A/B=2-368.
DR PDB; 3JZ6; X-ray; 1.90 A; A/B=2-368.
DR PDBsum; 3DTF; -.
DR PDBsum; 3DTG; -.
DR PDBsum; 3JZ6; -.
DR AlphaFoldDB; A0R066; -.
DR SMR; A0R066; -.
DR STRING; 246196.MSMEI_4176; -.
DR PRIDE; A0R066; -.
DR EnsemblBacteria; ABK74679; ABK74679; MSMEG_4276.
DR EnsemblBacteria; AFP40633; AFP40633; MSMEI_4176.
DR GeneID; 66735622; -.
DR KEGG; msg:MSMEI_4176; -.
DR KEGG; msm:MSMEG_4276; -.
DR PATRIC; fig|246196.19.peg.4197; -.
DR eggNOG; COG0115; Bacteria.
DR OMA; LTEVFAC; -.
DR OrthoDB; 1275805at2; -.
DR BRENDA; 2.6.1.42; 3512.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR EvolutionaryTrace; A0R066; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:UniProtKB.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0018272; P:protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine; IDA:UniProtKB.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Isopeptide bond;
KW Pyridoxal phosphate; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..368
FT /note="Branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000396109"
FT BINDING 101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:20445230"
FT BINDING 209
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:20445230"
FT BINDING 271..272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 314
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:20445230"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT CROSSLNK 299
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:3DTG"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 162..174
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3JZ6"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3DTG"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:3DTG"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:3DTG"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:3DTG"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3DTG"
SQ SEQUENCE 368 AA; 39837 MW; 19C86C028296591D CRC64;
MNSGPLEFTV SANTNPATDA VRESILANPG FGKYYTDHMV SIDYTVDEGW HNAQVIPYGP
IQLDPSAIVL HYGQEIFEGL KAYRWADGSI VSFRPEANAA RLQSSARRLA IPELPEEVFI
ESLRQLIAVD EKWVPPAGGE ESLYLRPFVI ATEPGLGVRP SNEYRYLLIA SPAGAYFKGG
IKPVSVWLSH EYVRASPGGT GAAKFGGNYA ASLLAQAQAA EMGCDQVVWL DAIERRYVEE
MGGMNLFFVF GSGGSARLVT PELSGSLLPG ITRDSLLQLA TDAGFAVEER KIDVDEWQKK
AGAGEITEVF ACGTAAVITP VSHVKHHDGE FTIADGQPGE ITMALRDTLT GIQRGTFADT
HGWMARLN
