ID   S8F550_TOXGM            Unreviewed;       636 AA.
AC   S8F550;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=TGME49_264030 {ECO:0000313|EMBL:EPT29792.1};
OS   Toxoplasma gondii (strain ATCC 50611 / Me49).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=508771 {ECO:0000313|EMBL:EPT29792.1, ECO:0000313|Proteomes:UP000001529};
RN   [1] {ECO:0000313|EMBL:EPT29792.1, ECO:0000313|Proteomes:UP000001529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50611 / Me49 {ECO:0000313|Proteomes:UP000001529};
RA   Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA   Roos D., Caler E., Lorenzi H.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   EMBL; KE138830; EPT29792.1; -; Genomic_DNA.
DR   RefSeq; XP_002365493.1; XM_002365452.1.
DR   AlphaFoldDB; S8F550; -.
DR   EnsemblProtists; TGME49_264030-t26_1; TGME49_264030-t26_1; TGME49_264030.
DR   GeneID; 7894795; -.
DR   KEGG; tgo:TGME49_264030; -.
DR   VEuPathDB; ToxoDB:TGME49_264030; -.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OrthoDB; 5472891at2759; -.
DR   PhylomeDB; S8F550; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001529; Chromosome VIIb.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF373; ALANINE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EPT29792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001529};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPT29792.1}.
FT   DOMAIN          237..611
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          56..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  70679 MW;  D031DF9CF370EAF5 CRC64;
     MQFFHLFDSL NSPFVCAYRK RFFIGVFGRS QFVSTKQHFS MMPKFVRGRA APMPETLEGV
     NSSCPAKTSN GSLPQSVAPA PSNPVNAENP PPQSAIATME THCRENGSGT LLHRHRSHLA
     DDVDMENRHR LSRQPTLSMC SLPERVVECK YAVRGVTVRR ALELQEQLTK SPNCLNFKKL
     IFANIGDPQA LGQRPISFYR QVMACVMYPP LVGLPLGCNR VELADIEPKN GQNTSFEENN
     SSSEEHTLFA LDIVAKSRRY LQAMGSVGAY THSQGHPLFR KDIAAWLTDR DGVATDPDTI
     FLTDGASSGI RLVLELLLRE RSDGLLIPVP QYPLYAGLIV RLGGRVVPYY LEEETGWSFS
     LSAVREAMQD AKRKGICVRG IVVINPGNPT GTVLTEKEIR EIINFCDTER LVLLADEVYQ
     DNVYGNVPFI SARKVLHQMD ANVSLFSFHS SSKGLVGECG LRGGLLHVDT ITEDVRLQMY
     KLVSMFMCGN TLGQLAITCV CTPPKPGDAS YERFQRERLA IYDSMKSKAH LVYDQLNQIE
     GVSCQPIAGA VFGFPQIRIP PGALREAKKK GVEADLLFCL ELLEATGIVT VPGSGFGQKH
     GTYHIRICIL PPKHVLVDML EKLKEFYAMF VKKYSE
//