ID   A0A0R3W9S1_TAEAS        Unreviewed;       416 AA.
AC   A0A0R3W9S1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial {ECO:0000256|ARBA:ARBA00040891};
DE   AltName: Full=Kynurenine aminotransferase 4 {ECO:0000256|ARBA:ARBA00041257};
DE   AltName: Full=Kynurenine aminotransferase IV {ECO:0000256|ARBA:ARBA00042891};
DE   AltName: Full=Kynurenine--oxoglutarate transaminase 4 {ECO:0000256|ARBA:ARBA00042867};
DE   AltName: Full=Kynurenine--oxoglutarate transaminase IV {ECO:0000256|ARBA:ARBA00041746};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000722601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000722601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   AlphaFoldDB; A0A0R3W9S1; -.
DR   STRING; 60517.A0A0R3W9S1; -.
DR   WBParaSite; TASK_0000722601-mRNA-1; TASK_0000722601-mRNA-1; TASK_0000722601.
DR   Proteomes; UP000046400; Unplaced.
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; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          43..411
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   416 AA;  46794 MW;  1CCAD65C4F55B227 CRC64;
     LLTSQILFRF RTNLRKMWSH VEMGPPDFVL GITEAFKRDT NPNKVNLGVG AYRDDNCKPW
     VLPSVREAEE RILSRHLDHE YLPISGLAPF CKAAIEFALG ADCPALKEGR NATVQCLSGT
     GSLRIGAAFL GRFSKVKEVY MPKPTWANHI PVFRDSGIAI QYYRYYDPKT CGLDEAGWLE
     DISHIPEGSI ILLHACAHNP TGVDPNHEQW KRAGKIIKER GLIPFFDMAY QGFASGNPDH
     DAWALRYFVN ELHPKTLFLA QSFAKNMGLY GERCGAFTLI CESKDEAERC MSQIKILIRP
     IISNPPLYGA RIASEILGDP DLKAKWMVDL KSMADRIIGV RKTLREELAK AGSKRNWEHI
     TNQIGMFCYT GLQPEQTERL TKEFSIYLTK DGRISMAGVT SKNVAYVAQA IHAVTK
//