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Entry: A0A1G5AZ19_9FIRM
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ID   A0A1G5AZ19_9FIRM        Unreviewed;       353 AA.
AC   A0A1G5AZ19;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE            EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN   ORFNames=SAMN02910371_00109 {ECO:0000313|EMBL:SCX83173.1};
OS   Butyrivibrio sp. INlla14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCX83173.1, ECO:0000313|Proteomes:UP000199551};
RN   [1] {ECO:0000313|Proteomes:UP000199551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; FMVS01000002; SCX83173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5AZ19; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000199551; Unassembled WGS sequence.
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: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; cd01557; BCAT_beta_family; 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; 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   NCBIfam; TIGR01123; ilvE_II; 1.
DR   PANTHER; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42825:SF7; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:SCX83173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199551};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCX83173.1}.
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   353 AA;  38849 MW;  719DE19F8712B149 CRC64;
     MHLSFGRGYK MSKKNLDWAN IGFGYMVADK RYVSNYKDGK WDEGTLTTDS TVTLSEDAGV
     LHYAQECFEG LKAYETEDGK IVTFRPDLNA KRMVDSAERL EMPSFPEDRF IKAVEEVVAA
     NKDWVPPYGS GATLYIRPVM FATGNVIGVK PADEYQFRIF VTPVGPYFKG GAKPIVVKIS
     DYDRAAPHGT GNIKAGLNYA MSLHAIVTAH EEGFAENVYL DAESRTYIEE TGGANIIFVT
     KDGGLVVPKS HTDSILPSIT RRSIVYVARE ILGMNVEERP VKLSEVSDFV EMGLCGTAAV
     ISPVGKINDH GKEICFASGM DEMGPVMKKL YDTLTGIQMG TVEAPEGWIH VIE
//
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