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Database: UniProt
Entry: A0A556QMJ4_9BACT
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ID   A0A556QMJ4_9BACT        Unreviewed;       274 AA.
AC   A0A556QMJ4;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE            EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN   ORFNames=FPL22_00750 {ECO:0000313|EMBL:TSJ77869.1};
OS   Rariglobus hedericola.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Rariglobus.
OX   NCBI_TaxID=2597822 {ECO:0000313|EMBL:TSJ77869.1, ECO:0000313|Proteomes:UP000315648};
RN   [1] {ECO:0000313|EMBL:TSJ77869.1, ECO:0000313|Proteomes:UP000315648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53C-WASEF {ECO:0000313|EMBL:TSJ77869.1,
RC   ECO:0000313|Proteomes:UP000315648};
RA   Pitt A., Hahn M.W.;
RT   "Description of 53C-WASEF.";
RL   Submitted (JUL-2019) 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:TSJ77869.1}.
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DR   EMBL; VMBG01000001; TSJ77869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A556QMJ4; -.
DR   OrthoDB; 9805628at2; -.
DR   Proteomes; UP000315648; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase 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   Aminotransferase {ECO:0000313|EMBL:TSJ77869.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000315648};
KW   Transferase {ECO:0000313|EMBL:TSJ77869.1}.
SQ   SEQUENCE   274 AA;  29286 MW;  1B4D8ED68D659484 CRC64;
     MTDASSQVIL DGVLLPAASA FIPATSEGFL YGHGIFETVK ITSGRPAFLA QHHARLTASA
     RALDLRYTVS IETLRERLAL VTTANTLTDG SVKIVLFARD ETTTGELIST KANAYPLETY
     ARGFRVNTVF TGERTGALSG HKTLNYLANI RAKRVAVAAG FDEPLFLTPA GIVIEGATSN
     IFTVRDGIAH TPSLASGPLP GIARAQVLAL LGSARVREGL LTHSDLLHAD EVFVTNALLG
     VMPVTQIDDR HLEIGPLTRS LKNLYHISET QSLS
//
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