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Database: UniProt
Entry: A0A443S6L5_9ACAR
LinkDB: A0A443S6L5_9ACAR
Original site: A0A443S6L5_9ACAR 
ID   A0A443S6L5_9ACAR        Unreviewed;       378 AA.
AC   A0A443S6L5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE            EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN   ORFNames=B4U80_00504 {ECO:0000313|EMBL:RWS23151.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS23151.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS23151.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS23151.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
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   -!- 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   -!- 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:RWS23151.1}.
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DR   EMBL; NCKV01007010; RWS23151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443S6L5; -.
DR   STRING; 299467.A0A443S6L5; -.
DR   EnsemblMetazoa; LDEU008889-RA; LDEU008889-PA; LDEU008889.
DR   VEuPathDB; VectorBase:LDEU008889; -.
DR   Proteomes; UP000288716; Unassembled WGS sequence.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
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; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR11825:SF44; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 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|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000313|EMBL:RWS23151.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW   Transferase {ECO:0000313|EMBL:RWS23151.1}.
SQ   SEQUENCE   378 AA;  43482 MW;  CCD84BA89C15DE81 CRC64;
     MNLASFMLVI FTKFTFESNF IDALEVGEPY PFSCVFSFKN STWEKPKMLN SPTGEISFLN
     KGIAIANSIV DSFRWFVGYD GEVRIFRPDF KLDRLNYGSQ KMNLEEIPKS YFYRCLNLFV
     EEARNRNMLP DPLKNQSIYT FSIYAASRAS NFVEQASETI FRLTGQMSNK LFHWKHATLK
     ARIEPDNFKN IGSFLAQYKA TSNYGISYVA DAIAKKSNYT TTLFLYPKTK RRKCLADLSN
     ANLFIVFRNK KGHTLVTLHD DHTLYAGSYR NSVITISQMI QNLRFKKRCV DVEMLQALVN
     SGQIVEMFSS GNSAQITPIT EISYKGEIIK IPTVQQSNPV YLQINNILYD IFYGLTKNAL
     FHEWMFCITA NGNDLQKC
//
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