BCAT2_HUMAN
ID BCAT2_HUMAN Reviewed; 392 AA.
AC O15382; B2RB87; O00269; Q96KG1; Q9BTB6; Q9BUU6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial {ECO:0000303|PubMed:9165094};
DE Short=BCAT(m) {ECO:0000303|PubMed:9165094};
DE EC=2.6.1.42 {ECO:0000269|PubMed:8702755};
DE AltName: Full=Placental protein 18 {ECO:0000303|PubMed:11170829};
DE Short=PP18 {ECO:0000303|PubMed:11170829};
DE Flags: Precursor;
GN Name=BCAT2;
GN Synonyms=BCATM {ECO:0000303|PubMed:9165094}, BCT2,
GN ECA40 {ECO:0000303|PubMed:8702755};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT ARG-186.
RX PubMed=9165094; DOI=10.1016/s0167-4838(97)00044-7;
RA Bledsoe R.K., Dawson P.A., Hutson S.M.;
RT "Cloning of the rat and human mitochondrial branched chain
RT aminotransferases (BCATm).";
RL Biochim. Biophys. Acta 1339:9-13(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11170829; DOI=10.1053/plac.2000.0603;
RA Than N.G., Sumegi B., Than G.N., Bellyei S., Bohn H.;
RT "Molecular cloning and characterization of placental tissue protein 18
RT (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its
RT novel alternatively spliced PP18b variant.";
RL Placenta 22:235-243(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-392 (ISOFORM A), FUNCTION, CATALYTIC
RP ACTIVITY, AND VARIANT ARG-186.
RC TISSUE=Brain;
RX PubMed=8702755; DOI=10.1074/jbc.271.34.20242;
RA Eden A., Simchen G., Benvenisty N.;
RT "Two yeast homologs of ECA39, a target for c-Myc regulation, code for
RT cytosolic and mitochondrial branched-chain amino acid aminotransferases.";
RL J. Biol. Chem. 271:20242-20245(1996).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INVOLVEMENT IN HVLI, VARIANTS HVLI GLN-170 AND LYS-264, AND FUNCTION.
RX PubMed=25653144; DOI=10.1007/s10545-015-9814-z;
RA Wang X.L., Li C.J., Xing Y., Yang Y.H., Jia J.P.;
RT "Hypervalinemia and hyperleucine-isoleucinemia caused by mutations in the
RT branched-chain-amino-acid aminotransferase gene.";
RL J. Inherit. Metab. Dis. 38:855-861(2015).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-392 IN COMPLEX WITH COFACTOR,
RP AND SUBUNIT.
RX PubMed=11264579; DOI=10.1107/s0907444901001925;
RA Yennawar N.H., Dunbar J., Conway M.E., Hutson S.M., Farber G.K.;
RT "The structure of human mitochondrial branched-chain aminotransferase.";
RL Acta Crystallogr. D 57:506-515(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR
RP AND SUBSTRATES.
RX PubMed=12269802; DOI=10.1021/bi020221c;
RA Yennawar N.H., Conway M.E., Yennawar H.P., Farber G.K., Hutson S.M.;
RT "Crystal structures of human mitochondrial branched chain aminotransferase
RT reaction intermediates: ketimine and pyridoxamine phosphate forms.";
RL Biochemistry 41:11592-11601(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR
RP AND SUBSTRATE ANALOGS.
RX PubMed=16141215; DOI=10.1074/jbc.m506486200;
RA Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam M.M.,
RA Hutson S.M.;
RT "Structural determinants for branched-chain aminotransferase isozyme-
RT specific inhibition by the anticonvulsant drug gabapentin.";
RL J. Biol. Chem. 280:37246-37256(2005).
RN [14] {ECO:0007744|PDB:2HDK, ECO:0007744|PDB:2HG8, ECO:0007744|PDB:2HGW, ECO:0007744|PDB:2HGX, ECO:0007744|PDB:2HHF}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-392 IN COMPLEXES WITH COFACTOR
RP AND SUBSTRATE ANALOGS, FUNCTION, AND MUTAGENESIS OF CYS-342 AND CYS-345.
RX PubMed=17050531; DOI=10.1074/jbc.m607552200;
RA Yennawar N.H., Islam M.M., Conway M., Wallin R., Hutson S.M.;
RT "Human mitochondrial branched chain aminotransferase isozyme: structural
RT role of the CXXC center in catalysis.";
RL J. Biol. Chem. 281:39660-39671(2006).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine
CC (PubMed:8702755, PubMed:25653144, PubMed:17050531). May also function
CC as a transporter of branched chain alpha-keto acids (By similarity).
CC {ECO:0000250|UniProtKB:O35854, ECO:0000269|PubMed:17050531,
CC ECO:0000269|PubMed:25653144, ECO:0000269|PubMed:8702755}.
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:0000269|PubMed:8702755};
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:0000269|PubMed:8702755};
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:0000269|PubMed:8702755};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215,
CC ECO:0000269|PubMed:17050531};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11264579}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O35854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O15382-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O15382-2; Sequence=VSP_000236;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11170829}.
CC -!- DISEASE: Hypervalinemia and hyperleucine-isoleucinemia (HVLI)
CC [MIM:618850]: An autosomal recessive metabolic disorder characterized
CC by highly elevated plasma concentrations of valine and
CC leucine/isoleucine. Affected individuals suffer from headache and mild
CC memory impairment. {ECO:0000269|PubMed:25653144}. Note=The disease is
CC caused by variants affecting the gene represented in this entry. A
CC patient with hypervalinemia and hyperleucine-isoleucinemia was
CC identified as compound heterozygote for Gln-170 (inherited from his
CC father) and Lys-264 (inherited from his mother), both variants reduced
CC the catalytic activity of the enzyme. After treatment with vitamin B6,
CC a precursor of pyridoxal 5'-phosphate, a BCAT2 cofactor, the blood
CC levels of branched chain amino acids, especially valine, were decreased
CC and brain lesions were improved. {ECO:0000269|PubMed:25653144}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53087.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U68418; AAB67672.1; -; mRNA.
DR EMBL; AF268047; AAK38368.1; -; mRNA.
DR EMBL; AF268048; AAK38369.1; -; mRNA.
DR EMBL; AK314548; BAG37134.1; -; mRNA.
DR EMBL; CH471177; EAW52403.1; -; Genomic_DNA.
DR EMBL; BC001900; AAH01900.1; -; mRNA.
DR EMBL; BC004243; AAH04243.2; -; mRNA.
DR EMBL; U62739; AAB53087.1; ALT_INIT; mRNA.
DR CCDS; CCDS12735.1; -. [O15382-1]
DR CCDS; CCDS54290.1; -. [O15382-2]
DR RefSeq; NP_001158245.1; NM_001164773.1. [O15382-2]
DR RefSeq; NP_001181.2; NM_001190.3. [O15382-1]
DR RefSeq; NP_001271254.1; NM_001284325.1.
DR PDB; 1EKF; X-ray; 1.95 A; A/B=28-392.
DR PDB; 1EKP; X-ray; 2.50 A; A/B=28-392.
DR PDB; 1EKV; X-ray; 2.25 A; A/B=28-392.
DR PDB; 1KT8; X-ray; 1.90 A; A/B=28-392.
DR PDB; 1KTA; X-ray; 1.90 A; A/B=28-392.
DR PDB; 2A1H; X-ray; 1.80 A; A/B=28-392.
DR PDB; 2HDK; X-ray; 2.40 A; A/B=28-392.
DR PDB; 2HG8; X-ray; 1.80 A; A/B=28-392.
DR PDB; 2HGW; X-ray; 1.98 A; A/B=28-392.
DR PDB; 2HGX; X-ray; 1.80 A; A/B=28-392.
DR PDB; 2HHF; X-ray; 1.80 A; A/B=28-392.
DR PDB; 5BWR; X-ray; 2.20 A; A/B=28-392.
DR PDB; 5BWT; X-ray; 2.20 A; A/B=28-392.
DR PDB; 5BWU; X-ray; 2.17 A; A/B=28-392.
DR PDB; 5BWV; X-ray; 1.86 A; A/B=28-392.
DR PDB; 5BWW; X-ray; 1.82 A; A/B=28-392.
DR PDB; 5BWX; X-ray; 1.70 A; A/B=28-392.
DR PDB; 5CR5; X-ray; 1.61 A; A/B=28-392.
DR PDB; 5HNE; X-ray; 2.04 A; A/B=28-392.
DR PDB; 5I5S; X-ray; 2.06 A; A/B=28-392.
DR PDB; 5I5T; X-ray; 2.31 A; A/B=28-392.
DR PDB; 5I5U; X-ray; 2.40 A; A/B=28-392.
DR PDB; 5I5V; X-ray; 1.94 A; A/B=28-392.
DR PDB; 5I5W; X-ray; 2.40 A; A/B=28-392.
DR PDB; 5I5X; X-ray; 1.65 A; A/B=28-392.
DR PDB; 5I5Y; X-ray; 1.81 A; A/B=28-392.
DR PDB; 5I60; X-ray; 2.12 A; A/B=28-392.
DR PDB; 5MPR; X-ray; 1.60 A; A=28-392.
DR PDB; 6PRX; X-ray; 3.25 A; A/B=28-392.
DR PDBsum; 1EKF; -.
DR PDBsum; 1EKP; -.
DR PDBsum; 1EKV; -.
DR PDBsum; 1KT8; -.
DR PDBsum; 1KTA; -.
DR PDBsum; 2A1H; -.
DR PDBsum; 2HDK; -.
DR PDBsum; 2HG8; -.
DR PDBsum; 2HGW; -.
DR PDBsum; 2HGX; -.
DR PDBsum; 2HHF; -.
DR PDBsum; 5BWR; -.
DR PDBsum; 5BWT; -.
DR PDBsum; 5BWU; -.
DR PDBsum; 5BWV; -.
DR PDBsum; 5BWW; -.
DR PDBsum; 5BWX; -.
DR PDBsum; 5CR5; -.
DR PDBsum; 5HNE; -.
DR PDBsum; 5I5S; -.
DR PDBsum; 5I5T; -.
DR PDBsum; 5I5U; -.
DR PDBsum; 5I5V; -.
DR PDBsum; 5I5W; -.
DR PDBsum; 5I5X; -.
DR PDBsum; 5I5Y; -.
DR PDBsum; 5I60; -.
DR PDBsum; 5MPR; -.
DR PDBsum; 6PRX; -.
DR AlphaFoldDB; O15382; -.
DR SMR; O15382; -.
DR BioGRID; 107062; 37.
DR IntAct; O15382; 11.
DR STRING; 9606.ENSP00000322991; -.
DR BindingDB; O15382; -.
DR ChEMBL; CHEMBL3616354; -.
DR DrugBank; DB04074; alpha-Ketoisovalerate.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00167; Isoleucine.
DR DrugBank; DB00149; Leucine.
DR DrugBank; DB02635; N-[O-Phosphono-Pyridoxyl]-Isoleucine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR GuidetoPHARMACOLOGY; 2893; -.
DR iPTMnet; O15382; -.
DR MetOSite; O15382; -.
DR PhosphoSitePlus; O15382; -.
DR BioMuta; BCAT2; -.
DR EPD; O15382; -.
DR jPOST; O15382; -.
DR MassIVE; O15382; -.
DR MaxQB; O15382; -.
DR PaxDb; O15382; -.
DR PeptideAtlas; O15382; -.
DR PRIDE; O15382; -.
DR ProteomicsDB; 48623; -. [O15382-1]
DR ProteomicsDB; 48624; -. [O15382-2]
DR Antibodypedia; 31810; 273 antibodies from 31 providers.
DR DNASU; 587; -.
DR Ensembl; ENST00000316273.11; ENSP00000322991.5; ENSG00000105552.15. [O15382-1]
DR Ensembl; ENST00000545387.6; ENSP00000440973.1; ENSG00000105552.15. [O15382-2]
DR GeneID; 587; -.
DR KEGG; hsa:587; -.
DR MANE-Select; ENST00000316273.11; ENSP00000322991.5; NM_001190.4; NP_001181.2.
DR UCSC; uc002pkr.4; human. [O15382-1]
DR CTD; 587; -.
DR DisGeNET; 587; -.
DR GeneCards; BCAT2; -.
DR HGNC; HGNC:977; BCAT2.
DR HPA; ENSG00000105552; Low tissue specificity.
DR MalaCards; BCAT2; -.
DR MIM; 113530; gene.
DR MIM; 618850; phenotype.
DR neXtProt; NX_O15382; -.
DR OpenTargets; ENSG00000105552; -.
DR PharmGKB; PA25289; -.
DR VEuPathDB; HostDB:ENSG00000105552; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR InParanoid; O15382; -.
DR OMA; GTAWFIT; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; O15382; -.
DR TreeFam; TF300882; -.
DR BRENDA; 2.6.1.42; 2681.
DR PathwayCommons; O15382; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; O15382; -.
DR SignaLink; O15382; -.
DR BioGRID-ORCS; 587; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; BCAT2; human.
DR EvolutionaryTrace; O15382; -.
DR GenomeRNAi; 587; -.
DR Pharos; O15382; Tchem.
DR PRO; PR:O15382; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O15382; protein.
DR Bgee; ENSG00000105552; Expressed in right adrenal gland cortex and 186 other tissues.
DR ExpressionAtlas; O15382; baseline and differential.
DR Genevisible; O15382; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IDA:UniProtKB.
DR GO; GO:0052654; F:L-leucine transaminase activity; IDA:UniProtKB.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IDA:UniProtKB.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; TAS:ProtInc.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006550; P:isoleucine catabolic process; IEA:Ensembl.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010817; P:regulation of hormone levels; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Branched-chain amino acid biosynthesis; Disease variant;
KW Lipid metabolism; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:O35854"
FT CHAIN 28..392
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001271"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12269802,
FT ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531"
FT MOD_RES 229
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:16141215,
FT ECO:0000269|PubMed:17050531, ECO:0007744|PDB:2A1H,
FT ECO:0007744|PDB:2HDK, ECO:0007744|PDB:2HG8,
FT ECO:0007744|PDB:2HGW, ECO:0007744|PDB:2HGX,
FT ECO:0007744|PDB:2HHF"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 9..100
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11170829"
FT /id="VSP_000236"
FT VARIANT 170
FT /note="R -> Q (in HVLI; reduced catalytic activity;
FT dbSNP:rs749866079)"
FT /evidence="ECO:0000269|PubMed:25653144"
FT /id="VAR_084533"
FT VARIANT 186
FT /note="T -> R (in dbSNP:rs11548193)"
FT /evidence="ECO:0000269|PubMed:8702755,
FT ECO:0000269|PubMed:9165094"
FT /id="VAR_048234"
FT VARIANT 264
FT /note="E -> K (in HVLI; reduced catalytic activity;
FT dbSNP:rs767653663)"
FT /evidence="ECO:0000269|PubMed:25653144"
FT /id="VAR_084534"
FT MUTAGEN 342
FT /note="C->A: Reduces activity about 6-fold."
FT /evidence="ECO:0000269|PubMed:17050531"
FT MUTAGEN 345
FT /note="C->A: Slight reduction of activity."
FT /evidence="ECO:0000269|PubMed:17050531"
FT CONFLICT 154
FT /note="V -> L (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="T -> N (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..216
FT /note="DPA -> EPT (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="L -> F (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> P (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="G -> A (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="R -> G (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="L -> F (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="L -> F (in Ref. 6; AAB53087)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2HG8"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1EKF"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5CR5"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1EKP"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2HG8"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5BWX"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:5MPR"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:5MPR"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:5MPR"
FT HELIX 367..380
FT /evidence="ECO:0007829|PDB:5MPR"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5MPR"
SQ SEQUENCE 392 AA; 44288 MW; EC07047264B190DA CRC64;
MAAAALGQIW ARKLLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG PGEPLVFGKT
FTDHMLMVEW NDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ LFEGMKAFKG KDQQVRLFRP
WLNMDRMLRS AMRLCLPSFD KLELLECIRR LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL
GVSQPTRALL FVILCPVGAY FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV
QQEALKRGCE QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS
LLDMAQTWGE FRVVERTITM KQLLRALEEG RVREVFGSGT ACQVCPVHRI LYKDRNLHIP
TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV
