UniProt: A0A087SNL4

Database: UniProt
Entry: A0A087SNL4_AUXPR

LinkDB:  A0A087SNL4_AUXPR 
Original site:  A0A087SNL4_AUXPR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (7)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A0A087SNL4_AUXPR        Unreviewed;       370 AA.
AC   A0A087SNL4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   ORFNames=F751_4588 {ECO:0000313|EMBL:KFM27318.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM27318.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM27318.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM27318.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
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|RuleBase:RU004517};
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|RuleBase:RU004517};
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|RuleBase:RU004517};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
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DR   EMBL; KL662144; KFM27318.1; -; Genomic_DNA.
DR   RefSeq; XP_011400285.1; XM_011401983.1.
DR   AlphaFoldDB; A0A087SNL4; -.
DR   STRING; 3075.A0A087SNL4; -.
DR   GeneID; 23615979; -.
DR   KEGG; apro:F751_4588; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   OrthoDB; 1304at2759; -.
DR   Proteomes; UP000028924; 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
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; 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; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42825:SF2; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU004517};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}.
SQ   SEQUENCE   370 AA;  39326 MW;  8144496990E223F6 CRC64;
     MALAHQLQLH QIGCLHRNAA ALRATPRPSL ARTVAKAVTE TEAVGAPTSS IDWDNLGFGI
     QGVAPSMFVA TFDTEMGEWS EGGVQPYGPL PMYPSAQVLN YGQAIFEGLK AQRSTRDRIV
     LFRPTSNAER MQAGAARMSM AAPPEDLFVR GVEAAVRSNA SYVPPQGKGS LYLRPLLIGS
     GPILGVGPAP SYTFIVYAAS VGAYFKGGQL SPIDLLVETR PGLGSLAAAK AEGYSDVLYL
     DAKHDNFLEE VSSCNVFAVY GKTIRTPPLA GTILPGVTRR SVIELARAKG YTVEEAPVSV
     AEALAADEVF TTGTAVVLCS VGSLTYQGTK QRYGTEGQPG PVALELYEAL TGLQQERTED
     PFGWVHHVPL
//

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