ID   BCAT_NEMVE              Reviewed;         405 AA.
AC   A7SLW1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase;
DE            EC=2.6.1.42;
GN   ORFNames=v1g246094;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC       essential branched chain amino acids leucine, isoleucine, and valine.
CC       {ECO:0000250}.
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   -!- 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   -!- 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; DS469702; EDO35327.1; -; Genomic_DNA.
DR   RefSeq; XP_001627427.1; XM_001627377.1.
DR   AlphaFoldDB; A7SLW1; -.
DR   SMR; A7SLW1; -.
DR   STRING; 45351.EDO35327; -.
DR   EnsemblMetazoa; EDO35327; EDO35327; NEMVEDRAFT_v1g246094.
DR   GeneID; 5506714; -.
DR   KEGG; nve:5506714; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   HOGENOM; CLU_031922_0_3_1; -.
DR   InParanoid; A7SLW1; -.
DR   OMA; PVGSYYK; -.
DR   OrthoDB; 853728at2759; -.
DR   PhylomeDB; A7SLW1; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
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:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   Gene3D; 3.20.10.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 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   PANTHER; PTHR11825; PTHR11825; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..405
FT                   /note="Branched-chain-amino-acid aminotransferase"
FT                   /id="PRO_0000340238"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  45659 MW;  5FDD114D8C4E024B CRC64;
     MAARVGLLQT IGKLQSSFLY RAWPKHSINA KQLARQLSSY HDIKSSNLLI EKTNKPKPKP
     DPNTLVFGKE FTDHALILKW SDEDGWDNPQ IIPYGNLSLP PAASALHYGL ECFEGMKAYR
     GDDGKIRMFR PLMNMKRMNN SAARACLPTF NSGEMVECIR KLIHLEREWV PHSNTCSLYI
     RPTMIGTQAS LGVNKANSAM LFVILSPVGP YFRTGTFNPV ALLADPQYVR AWPGGVGDCK
     MGGNYAPTIL AQQNAERQGL QQVLWLFGED HQITEVGTMN MFMFWINENG EKELVTPPLN
     GLILPGVTRD SLLALAKRWG EFKVTERTFN MQDVLMATEE NRMLEMFGSG TACVVCPINR
     IFYQGKNIMI PTMENLNVTK RVYDELTGIQ YGRQEGPKDW IVMVD