ID A0A1R1RKH8_9BACI Unreviewed; 304 AA.
AC A0A1R1RKH8; A0A1R1QJD6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ilvE {ECO:0000256|RuleBase:RU364094};
GN ORFNames=BTA30_19210 {ECO:0000313|EMBL:OMI26511.1}, BW143_12965
GN {ECO:0000313|EMBL:OMI04771.1};
OS Bacillus swezeyi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI26511.1, ECO:0000313|Proteomes:UP000187536};
RN [1] {ECO:0000313|EMBL:OMI26511.1, ECO:0000313|Proteomes:UP000187536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMI04771.1,
RC ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC {ECO:0000313|EMBL:OMI26511.1, ECO:0000313|Proteomes:UP000187536};
RA Dunlap C.;
RT "Bacillus phylogenomics.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109, ECO:0000256|RuleBase:RU364094}.
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 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 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:OMI26511.1}.
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DR EMBL; MTJL01000024; OMI04771.1; -; Genomic_DNA.
DR EMBL; MRBK01000029; OMI26511.1; -; Genomic_DNA.
DR RefSeq; WP_076763069.1; NZ_MTJL01000024.1.
DR OrthoDB; 9805628at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000187367; Unassembled WGS sequence.
DR Proteomes; UP000187536; 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; cd01558; D-AAT_like; 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; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR NCBIfam; TIGR01122; ilvE_I; 1.
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 Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Aminotransferase {ECO:0000256|RuleBase:RU364094,
KW ECO:0000313|EMBL:OMI04771.1};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Transferase {ECO:0000256|RuleBase:RU364094}.
SQ SEQUENCE 304 AA; 34122 MW; 1CA38212C72BB0E6 CRC64;
MGDQKDQWIF LNDKLVKKED AKISVYDHGF LYGDGVFEGI RVYDGNIFRM KEHMDRLYDS
ARSILLKIPY QQEELTQYVL RTVEKNGLKD AYIRLVVSRG AGDLGLDPNN CSNPSVIIIV
EPLAIFPKHL YETGIDIVTV PTRRNRPDVL SPKVKSLNYL NNILVRIEAQ MAGVSEALML
NDQGYVAEGS ADNVFIYKNG KLLTPPGYIG ALEGITRNAI IEIAEELGYE VKEEPFTRHD
VYTADEVFLT GTAAEVIAVV KVDGRQIGDG KPGVHTNRML EKFRERVVRE GEKADIKDQS
LSVS
//
