ILVE_MYCTU
ID ILVE_MYCTU Reviewed; 368 AA.
AC P9WQ75; L0TBM2; Q10399;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
GN Name=ilvE; OrderedLocusNames=Rv2210c; ORFNames=MTCY190.21c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN AMINOTRANSFERASE, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH
RP PYRIDOXAMINE-5'-PHOSPHATE, AND SUBUNIT.
RX PubMed=19923721; DOI=10.1107/s1744309109036690;
RA Tremblay L.W., Blanchard J.S.;
RT "The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE)
RT from Mycobacterium tuberculosis.";
RL Acta Crystallogr. F 65:1071-1077(2009).
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-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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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:19923721}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44987.1; -; Genomic_DNA.
DR PIR; C70786; C70786.
DR RefSeq; NP_216726.1; NC_000962.3.
DR RefSeq; WP_003411438.1; NZ_NVQJ01000008.1.
DR PDB; 3HT5; X-ray; 1.90 A; A=1-368.
DR PDB; 5U3F; X-ray; 1.70 A; A/B=1-368.
DR PDBsum; 3HT5; -.
DR PDBsum; 5U3F; -.
DR AlphaFoldDB; P9WQ75; -.
DR SMR; P9WQ75; -.
DR STRING; 83332.Rv2210c; -.
DR PaxDb; P9WQ75; -.
DR PRIDE; P9WQ75; -.
DR DNASU; 888352; -.
DR GeneID; 45426186; -.
DR GeneID; 888352; -.
DR KEGG; mtu:Rv2210c; -.
DR TubercuList; Rv2210c; -.
DR eggNOG; COG0115; Bacteria.
DR OMA; LTEVFAC; -.
DR PhylomeDB; P9WQ75; -.
DR BRENDA; 2.6.1.42; 3445.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000001584; 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:MTBBASE.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:MTBBASE.
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:0071267; P:L-methionine salvage; IDA:MTBBASE.
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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..368
FT /note="Branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103274"
FT BINDING 101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 209
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
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 MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:5U3F"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3HT5"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 162..173
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:5U3F"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5U3F"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:5U3F"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:5U3F"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:5U3F"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5U3F"
SQ SEQUENCE 368 AA; 39666 MW; 3B16D3F81E234F4F CRC64;
MTSGSLQFTV LRAVNPATDA QRESMLREPG FGKYHTDHMV SIDYAEGRGW HNARVIPYGP
IELDPSAIVL HYAQEVFEGL KAYRWADGSI VSFRADANAA RLRSSARRLA IPELPDAVFI
ESLRQLIAVD KAWVPGAGGE EALYLRPFIF ATEPGLGVRP ATQYRYLLIA SPAGAYFKGG
IAPVSVWVST EYVRACPGGT GAAKFGGNYA ASLLAQAEAA ENGCDQVVWL DAVERRYIEE
MGGMNIFFVL GSGGSARLVT PELSGSLLPG ITRDSLLQLA IDAGFAVEER RIDIDEWQKK
AAAGEITEVF ACGTAAVITP VARVRHGASE FRIADGQPGE VTMALRDTLT GIQRGTFADT
HGWMARLG
