ILVE_SALTY
ID ILVE_SALTY Reviewed; 309 AA.
AC P0A1A5; P15168; Q9L6T0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=Transaminase B;
GN Name=ilvE; OrderedLocusNames=STM3903; ORFNames=STMD1.89;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-309.
RX PubMed=2669973; DOI=10.1021/bi00438a058;
RA Feild M.J., Nguyen D.C., Armstrong F.B.;
RT "Amino acid sequence of Salmonella typhimurium branched-chain amino acid
RT aminotransferase.";
RL Biochemistry 28:5306-5310(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-6.
RA Randall R.R., Wallis M.H., Young G.J., Armstrong F.B.;
RT "N-terminal sequence of branched-chain amino acid aminotransferase.";
RL Fed. Proc. 38:325-325(1979).
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
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 -!- 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: Homohexamer.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF233324; AAF33481.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22753.1; -; Genomic_DNA.
DR PIR; A34082; A34082.
DR RefSeq; NP_462794.1; NC_003197.2.
DR RefSeq; WP_000208528.1; NC_003197.2.
DR AlphaFoldDB; P0A1A5; -.
DR SMR; P0A1A5; -.
DR STRING; 99287.STM3903; -.
DR PaxDb; P0A1A5; -.
DR PRIDE; P0A1A5; -.
DR EnsemblBacteria; AAL22753; AAL22753; STM3903.
DR GeneID; 1255429; -.
DR KEGG; stm:STM3903; -.
DR PATRIC; fig|99287.12.peg.4125; -.
DR HOGENOM; CLU_020844_3_1_6; -.
DR OMA; LTEVFAC; -.
DR PhylomeDB; P0A1A5; -.
DR BioCyc; SENT99287:STM3903-MON; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
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:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01122; ilvE_I; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2669973, ECO:0000269|Ref.3"
FT CHAIN 2..309
FT /note="Branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103266"
FT MOD_RES 160
FT /note="N6-(pyridoxal phosphate)lysine"
SQ SEQUENCE 309 AA; 34053 MW; 4F60941F3D63CC69 CRC64;
MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV VFRHREHMQR
LRDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL VFVGDVGMGV NPPPGYTTDV
IIAAFPWGAY LGAEALDQGI DAMVSSWNRA APNTIPTAAK AGGNYLSSLL VGSEARRHGY
QEGIALDVNG YISEGAGENL FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ
VLSRESLYLA DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK
WGWLDPVNS
