ID   D8LWJ3_BLAHO            Unreviewed;       444 AA.
AC   D8LWJ3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=GSBLH_T00000552001 {ECO:0000313|EMBL:CBK20182.2};
OS   Blastocystis hominis.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK20182.2};
RN   [1] {ECO:0000313|EMBL:CBK20182.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK20182.2};
RA   Wincker P.;
RT   "Sequencing and annotation of the Blastocystis hominis genome.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000984,
CC         ECO:0000256|RuleBase:RU000480};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU000480}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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; FN668638; CBK20182.2; -; Genomic_DNA.
DR   RefSeq; XP_012894230.1; XM_013038776.1.
DR   AlphaFoldDB; D8LWJ3; -.
DR   EnsemblProtists; CBK20182; CBK20182; GSBLH_T00000552001.
DR   GeneID; 24917859; -.
DR   InParanoid; D8LWJ3; -.
DR   OMA; VGACTIV; -.
DR   OrthoDB; 1123851at2759; -.
DR   Proteomes; UP000008312; Unassembled WGS sequence.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          65..431
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   444 AA;  49986 MW;  3512782120363433 CRC64;
     MNRESWYKTR IGTRSKSIWL EGLNSLFIYS LIFHTNMSIW NDVPLGPPDA IFKVSTGYQN
     DTDPRKVNLG VGAYRTDEGK PYYFPVVRKA EERILADKSG NKEYLPIDGL PQFRDLASKF
     LLGETHPAIV EKRVCTVQSL SGTGALRLGA EFLKKYMSGR KVYLPDPTWG NHNAIFTETG
     FEVVKYRWYE AATCALDFAG LKEDLSNAPE GSIVLFHTCA HNPTGVDPTQ EQWQALAELC
     QSRKLVPFFD TAYQGFASGD LVRDGYSVRL FAERGMEMLA AQSFAKNMGL YGERIGSINL
     ICHDAETATR VQSQMKIIVR KMYSNPPMHG AKIVATILGD KELFAEWEKE LKEIVGRILL
     MRKSLHEALL ENGCPGTWDH ITKQIGMFSF TGLDPDQSDR MVNLHHIYML RTGRISLAGL
     TSGSVKYVAD CIKEVVEWKL NGKQ
//