ID A0A1Y5Y0I1_KIBAR Unreviewed; 363 AA.
AC A0A1Y5Y0I1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN ORFNames=DMH04_32275 {ECO:0000313|EMBL:RSM78958.1}, SAMN05661093_07843
GN {ECO:0000313|EMBL:SMD23269.1};
OS Kibdelosporangium aridum.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=2030 {ECO:0000313|EMBL:SMD23269.1, ECO:0000313|Proteomes:UP000192674};
RN [1] {ECO:0000313|EMBL:SMD23269.1, ECO:0000313|Proteomes:UP000192674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43828 {ECO:0000313|EMBL:SMD23269.1,
RC ECO:0000313|Proteomes:UP000192674};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RSM78958.1, ECO:0000313|Proteomes:UP000287547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A82846 {ECO:0000313|EMBL:RSM78958.1,
RC ECO:0000313|Proteomes:UP000287547};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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 ECO:0000256|RuleBase:RU004517};
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:RU004517};
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:RU004517};
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}.
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DR EMBL; QHKI01000034; RSM78958.1; -; Genomic_DNA.
DR EMBL; FWXV01000009; SMD23269.1; -; Genomic_DNA.
DR RefSeq; WP_033383615.1; NZ_QHKI01000034.1.
DR AlphaFoldDB; A0A1Y5Y0I1; -.
DR OrthoDB; 9804984at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000192674; Unassembled WGS sequence.
DR Proteomes; UP000287547; 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; IPR018300; Aminotrans_IV_CS.
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; PTHR11825:SF44; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 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|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU004517};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU004517};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000192674};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}.
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 363 AA; 39680 MW; 156594039CA57CC8 CRC64;
MTSTLSFTQT SSPNPATPER LAEVLANPGF GQHFTDHMVT IRWSNDQGWH SAELEPYHPL
TLDPAATVLH YGQAIFEGLK AYRHQDGSIV AFRPEANAER FQNSARRMAM PELPTALFIE
SLHQLLAVDG RWVPDRAEAS LYLRPFMISD ESTLGVNRPA NHYLYALIAS PAGPYFATGV
KPVKVWLCTD YVRAAPGGTG AAKCAGNYAA SFVAQAQAVE QGCDQVVWLD AVERRWVEEV
GAMNLFFVFG NRLVTPELSG SLLPGITRDS LLTLARDHGY TVEERRVSTE EWEKKAESGE
LTEVFGCGTA AVITPVGSVK STAGEFTIGG GQPGEVTMKL RQALNDLQRG AAPDPHNWLH
RLA
//
