ID A0A0W0SU49_9GAMM Unreviewed; 679 AA.
AC A0A0W0SU49;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU364094};
DE Short=BCAT {ECO:0000256|RuleBase:RU364094};
DE EC=2.6.1.42 {ECO:0000256|RuleBase:RU364094};
GN Name=ala_1 {ECO:0000313|EMBL:KTC86906.1};
GN Synonyms=ilvE {ECO:0000256|RuleBase:RU364094};
GN ORFNames=Lbru_0135 {ECO:0000313|EMBL:KTC86906.1};
OS Legionella brunensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC86906.1, ECO:0000313|Proteomes:UP000054742};
RN [1] {ECO:0000313|EMBL:KTC86906.1, ECO:0000313|Proteomes:UP000054742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC86906.1,
RC ECO:0000313|Proteomes:UP000054742};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109, ECO:0000256|RuleBase:RU364094}.
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC {ECO:0000256|ARBA:ARBA00037629}.
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 Evidence={ECO:0000256|ARBA:ARBA00000627,
CC ECO:0000256|RuleBase:RU364094};
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 Evidence={ECO:0000256|ARBA:ARBA00000995,
CC ECO:0000256|RuleBase:RU364094};
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 Evidence={ECO:0000256|ARBA:ARBA00001745,
CC ECO:0000256|RuleBase:RU364094};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004516};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004824, ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00005072,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTC86906.1}.
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DR EMBL; LNXV01000003; KTC86906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0SU49; -.
DR STRING; 29422.Lbru_0135; -.
DR PATRIC; fig|29422.6.peg.138; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000054742; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR CDD; cd00449; PLPDE_IV; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR000891; PYR_CT.
DR NCBIfam; TIGR01122; ilvE_I; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU364094};
KW Aminotransferase {ECO:0000256|RuleBase:RU364094,
KW ECO:0000313|EMBL:KTC86906.1};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU364094}; Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Transferase {ECO:0000256|RuleBase:RU003523, ECO:0000313|EMBL:KTC86906.1}.
FT DOMAIN 9..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 679 AA; 74387 MW; 26E5BD5A80D38DC8 CRC64;
MSVNTNEKII ILDTTLRDGE QAPGATMMVS QKIEIAEALD SMGVDIIEAG FAAASSGDFA
CIKQISRVVK NARVSSLARA KIPDIEAAGM AVKSAVNPRI HTFISTSDLH LKYQFRMTQE
DALAAVESSV KSARNFCDDV EWSAMDATRS NIDFLAKAVE MAINAGANTI NIPDTVGYTT
PDEYSDLIKA LKNKVANIDK VILSVHCHND LGLAVANSMA AIRAGARQIE CTINGIGERA
GNAALEEIVM TIKTRQDKFP FTMNINPTHI ATVSQMVSKA SGFTVQKNKA IVGANAFAHE
SGIHQDGMLK CRETYEIMTP ESVGFSQSKL SMGKHSGRAA FRNKLSALQM DVREDNFDEL
FNKFKKLGDS QKEVTDAEII ALAEGKKTTI QQEKGAIWID GQFVPWSDAH VPILTHALHY
ASAVFEGARA YNGKVFKLHE HNERLHASAK TLGFTIPYSI AELNSVTEEL LCRNHLQDAY
IRPIAWCGEE TMSVASHSCT IHVAIAAWSW KSYFSDERSM QTGLKLMWAD WIRPSPSTAP
VTAKAAGLYM IGSLSKNKAE QAGFHDALML DYRGFVAECT GANFFMVKNG VIHTPIADCF
LNGITRQTVI AIAKSHHIPI IERHIYPHEV TEADEVFITG SAVEIAPISQ IGEHSFKVGE
ITQRITQAYS NLVRGHDYD
//
