ID   B0EBN9_ENTDS            Unreviewed;       484 AA.
AC   B0EBN9;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=EDI_325280 {ECO:0000313|EMBL:EDR28051.1};
OS   Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN   [1] {ECO:0000313|Proteomes:UP000008076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA   Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT   "Annotation of Entamoeba dispar SAW760.";
RL   Submitted (DEC-2007) 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; DS548606; EDR28051.1; -; Genomic_DNA.
DR   RefSeq; XP_001735733.1; XM_001735681.1.
DR   AlphaFoldDB; B0EBN9; -.
DR   EnsemblProtists; EDR28051; EDR28051; EDI_325280.
DR   GeneID; 5880696; -.
DR   KEGG; edi:EDI_325280; -.
DR   VEuPathDB; AmoebaDB:EDI_325280; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   OMA; FGFECPP; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008076; Unassembled WGS sequence.
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:SF29; ALANINE TRANSAMINASE; 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:EDR28051.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDR28051.1}.
FT   DOMAIN          94..471
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   484 AA;  54895 MW;  294EE31A02A32FF2 CRC64;
     MKAFSRQSIN PCIIATQYAV RGKLVLEANG IQKEIEEAKK KGKTNPYPFD KVVYCNIGNP
     QICNQQPLTY PRQIISIVEY PELLNHTSFF PKDVINHAKK IINSLGCTGT SGAYTNSMGV
     VQFRKSICKF IKRRDGTAPS PDEVFITDGA STGIKMILNM LISHPLHGIM IPIPQYPLYS
     AAISQFGGFQ INYYLDESKK WSTDMTSVRK VYEQAVEKGI QVKGFVCINP GNPTGQVLTV
     QNMKEIIEFC YEKKICLLAD EVYQENIYGE IPFTSFRKVL KSMRDEVKNT VELVSFFSVS
     KGFYGECGKR GGYFQIENIN SFARSQMYKM ASINLCSNVI GQEMVEIICN PPKEGDESYP
     KYINEKMSIL NSLKRKAKLL HSVLNECEGI TCNEAMGALY LFPKIKFSNK YIDECKRKDQ
     QPDEVYCLRM LKSIGVCVVP GSGFGQKDNT YHFRIAILPP ENEIQNIANK IKIFHTSFMK
     EYDH
//