ID A0A0Q8YEM9_9MICO Unreviewed; 281 AA.
AC A0A0Q8YEM9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN ORFNames=ASE25_10775 {ECO:0000313|EMBL:KRC89981.1};
OS Terrabacter sp. Root85.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Terrabacter.
OX NCBI_TaxID=1736603 {ECO:0000313|EMBL:KRC89981.1, ECO:0000313|Proteomes:UP000051752};
RN [1] {ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|Proteomes:UP000051752};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC89981.1, ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|EMBL:KRC89981.1,
RC ECO:0000313|Proteomes:UP000051752};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109}.
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 -!- 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 -!- 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 -!- 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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005072}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC ECO:0000256|RuleBase:RU004106}.
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:KRC89981.1}.
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DR EMBL; LMIW01000008; KRC89981.1; -; Genomic_DNA.
DR RefSeq; WP_056825329.1; NZ_LMIW01000008.1.
DR AlphaFoldDB; A0A0Q8YEM9; -.
DR STRING; 1736603.ASE25_10775; -.
DR Proteomes; UP000051752; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd00449; PLPDE_IV; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42743:SF20; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-LIKE PROTEIN 2; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KRC89981.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516}.
SQ SEQUENCE 281 AA; 29764 MW; 1B20592108DED1B4 CRC64;
MSTTTRVWVN GDLVDPTGPS VSALDHSVTV GDGVFETAKI ASGVPFALTR HHRRLERSAT
GLGLPPLDLA VVDKGVAAVL DGPAIDFGRL RYSVTGGVGP LGSDRDDTAL TYIVLAAPQP
LPPSSGKLTV VPWTRNERSA VVGLKTTSYA ENVVAFARAK QVGAVEAVFG NTRGELCECT
GSNVFVVVDG VVLTPPAESG LLLGITRELT IEWGRAAGLE IREETLPLDV LRSADEVFIT
SSTKDVLPVH AVDDRDLSAD RPVTTELQRV FRSNAERDSD P
//
