ID   A0A183MJ50_9TREM        Unreviewed;       331 AA.
AC   A0A183MJ50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=SMRZ_LOCUS16075 {ECO:0000313|EMBL:VDP19906.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001607601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001607601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP19906.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDP19906.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UZAI01017057; VDP19906.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183MJ50; -.
DR   WBParaSite; SMRZ_0001607601-mRNA-1; SMRZ_0001607601-mRNA-1; SMRZ_0001607601.
DR   Proteomes; UP000277204; 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:UP000277204};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          69..326
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   331 AA;  37430 MW;  9D355226E754F05C CRC64;
     MVEPTGTYVP ANIARMGHHD RQARPPRQGS SFGRAIVKRL IESLNTNIQS MDDHFVCDCR
     NVYLFLKYRH SGLNVHQYRY YNSNTCGLDI DGCLSDLSKI PKGHFVLLHA CAHNPTGVDP
     SFEQWQKIGE ILQSRGLIPF FDCAYQGFAS GNIDNDARAI RYFTDELNFP TILLTQSFAK
     NMGLYGERVG AFTLLCSSPD EAERCLSQIK IIIRPMYSNP PIHGARIATE LMSNPDLRQK
     WLIDLKTMAD RIITMRQSLR NSLIKAGSHH DWSHITNQIG MFCYSGLNPS QVEKLTNEYS
     IYLTKDGRIS IAGLSSKNVD YLAHAIHQVT K
//