BCAT1_HUMLU
ID BCAT1_HUMLU Reviewed; 393 AA.
AC K7QKH1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Branched-chain amino acid aminotransferase 1, mitochondrial {ECO:0000303|PubMed:23347725};
DE Short=HlBCAT1 {ECO:0000303|PubMed:23347725};
DE EC=2.6.1.42 {ECO:0000269|PubMed:23347725};
DE Flags: Precursor;
GN Name=BCAT1 {ECO:0000303|PubMed:23347725};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23347725; DOI=10.1186/1471-2229-13-12;
RA Clark S.M., Vaitheeswaran V., Ambrose S.J., Purves R.W., Page J.E.;
RT "Transcriptome analysis of bitter acid biosynthesis and precursor pathways
RT in hop (Humulus lupulus).";
RL BMC Plant Biol. 13:12-12(2013).
CC -!- FUNCTION: Converts 2-oxo acids to branched-chain amino acids (BCAA).
CC Shows no kinetic preferences corresponding to anabolic or catabolic
CC functions, but likely involved in BCAA catabolism.
CC {ECO:0000269|PubMed:23347725}.
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:23347725};
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:23347725};
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:23347725};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|RuleBase:RU004516};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=720 uM for glutamate {ECO:0000269|PubMed:23347725};
CC KM=35 uM for ketoisocarpoate {ECO:0000269|PubMed:23347725};
CC KM=99 uM for ketoisomethylvalerate {ECO:0000269|PubMed:23347725};
CC KM=99 uM for ketoisovalerate {ECO:0000269|PubMed:23347725};
CC KM=30 uM for 2-oxoglutarate {ECO:0000269|PubMed:23347725};
CC KM=40 uM for leucine {ECO:0000269|PubMed:23347725};
CC KM=230 uM for isoleucine {ECO:0000269|PubMed:23347725};
CC KM=340 uM for valine {ECO:0000269|PubMed:23347725};
CC Vmax=5.59 umol/min/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=4.50 umol/min/mg enzyme with ketoisocarpoate as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=2.95 umol/min/mg enzyme with ketoisomethylvalerate as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=4.23 umol/min/mg enzyme with ketoisovalerate as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=4.50 umol/min/mg enzyme with 2-oxoglutarate as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=4.84 umol/min/mg enzyme with leucine as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=19.40 umol/min/mg enzyme with isoleucine as substrate
CC {ECO:0000269|PubMed:23347725};
CC Vmax=12.60 umol/min/mg enzyme with valine as substrate
CC {ECO:0000269|PubMed:23347725};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000305}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000305}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23347725}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in lupulin glands.
CC {ECO:0000269|PubMed:23347725}.
CC -!- MISCELLANEOUS: Branched-chain amino acids are synthesized in
CC chloroplasts, whereas the degradation takes place in mitochondria.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; JQ063073; AFU07634.1; -; mRNA.
DR AlphaFoldDB; K7QKH1; -.
DR SMR; K7QKH1; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 3.20.10.10; -; 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; PTHR42825; PTHR42825; 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 Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Mitochondrion; Pyridoxal phosphate;
KW Transferase; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..393
FT /note="Branched-chain amino acid aminotransferase 1,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439267"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 138
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 276
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 393 AA; 43182 MW; DFF27E6197BA0425 CRC64;
MIHRGLWLHN LVQSYRVGSS SSSSTLFKLV YRYNSSTSLA KSSLKQSCEL SCKSNTEPSN
MDWDKLGFKL MPTDYVYSMK CSNEGNFEQG RLELHGNIEL SPAAAVLNYG QGIFEGTKAY
RKEDGSLLLF RPDQNGVRMR IGAERMCMPS PSVDQFVDAV KQTAIANRRW VPPSGKGSLY
IRPLLMGTGA VLGVAPAPQY TFLAYASPVG NYFKEGLAPL RLYVEDEFDR ASPGGTGFVK
TIGNYSRCLA ALSRAKNKGF SDVLFLDSVH KKYVEELSSC NIFIVQGNQI STPAANGTIL
SGVTRSSIIE IARDHGFKVE ERKIAVDELM EAEEVFCTGT AVGVASVGSI TYHNKRVEFK
TGSQSVSQKF YSTLIGIQTG VVEDKKGWIV EID
