ID D8JSJ8_HYPDA Unreviewed; 298 AA.
AC D8JSJ8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Hden_2496 {ECO:0000313|EMBL:ADJ24292.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ24292.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002083; ADJ24292.1; -; Genomic_DNA.
DR RefSeq; WP_013216451.1; NC_014313.1.
DR AlphaFoldDB; D8JSJ8; -.
DR STRING; 582899.Hden_2496; -.
DR KEGG; hdn:Hden_2496; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_3_1_5; -.
DR OrthoDB; 21319at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000002033; Chromosome.
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:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
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 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:ADJ24292.1};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW Transferase {ECO:0000256|RuleBase:RU364094, ECO:0000313|EMBL:ADJ24292.1}.
SQ SEQUENCE 298 AA; 33449 MW; 9F23EE639E312F70 CRC64;
MADLVPYHDR DGLIWMDGAL LPWRDVKVHV LTHALHYASA VFEGERSYEG EIFKLTEHSE
RLVESAKILD FDIPYSVAEI DQACRDTVAA NKLSDCYVRP LAWRGSEQMG VSARQTKIHL
MVAAWNWGSY FPMEQRLKGI RITHAQYRRP DPACAPAKAK AAGLYMICTI EKHRAERAGY
SDALMLDYRG RVAECTGANV FLIKDGVIHT PEPDCFLDGI TRRTVIDLAK ARGIEVIARA
IMPEELGSFT ECFITGTAAE ITPVSEIGEH HYKPGKITET LLNDYTELVK PKKRVAAE
//