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Database: UniProt
Entry: A0A0A2WUD1_THEFI
LinkDB: A0A0A2WUD1_THEFI
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ID   A0A0A2WUD1_THEFI        Unreviewed;       316 AA.
AC   A0A0A2WUD1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=THFILI_11300 {ECO:0000313|EMBL:KGQ22382.1};
OS   Thermus filiformis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ22382.1, ECO:0000313|Proteomes:UP000030364};
RN   [1] {ECO:0000313|EMBL:KGQ22382.1, ECO:0000313|Proteomes:UP000030364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ22382.1,
RC   ECO:0000313|Proteomes:UP000030364};
RA   Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA   Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT   "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT   producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL   Submitted (FEB-2015) 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:RU364094};
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:RU364094}.
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:KGQ22382.1}.
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DR   EMBL; JPSL02000040; KGQ22382.1; -; Genomic_DNA.
DR   RefSeq; WP_038062845.1; NZ_JPSL02000040.1.
DR   AlphaFoldDB; A0A0A2WUD1; -.
DR   STRING; 276.THFILI_11300; -.
DR   PATRIC; fig|276.5.peg.799; -.
DR   OrthoDB; 9805628at2; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000030364; 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: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   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; IPR005785; B_amino_transI.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   NCBIfam; TIGR01122; ilvE_I; 1.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF11; AMINODEOXYCHORISMATE LYASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU364094};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU364094};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364094}.
SQ   SEQUENCE   316 AA;  34844 MW;  88B859E3001A45A8 CRC64;
     MSTQAQAKGG DTQIKAGLIW FNGRMVPQEE AKVSVLSHAL HYGTSVFEGI RAYETPKGPA
     IFRLQEHVDR FFNSAKVLRM ELPFSKEEVA EAIKEVVRQN GYKSCYIRPL AWMGARTLGV
     NPLPNNPAEV MVAAWEWGAY LGEEAVRKGA RLVTSSWARF PANVLPGKAK VGGNYVNSAL
     AKMEAVSAGA DEALLLDEEG YVAEGSGENV FFVRGGVVYA IEHSVNLEGI TRDSVIRIAK
     DLGYEVQVVR ATRDQLYMAD EMFITGTAAE VTPVAMLDWR PIGKGVAGEV TLRIRQAYLE
     AVTGRRPEYE HWLTYV
//
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