ID   A8BP13_GIAIC            Unreviewed;       479 AA.
AC   A8BP13;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=GL50803_0016363 {ECO:0000313|EMBL:KAE8304642.1},
GN   GL50803_16363 {ECO:0000313|EMBL:EDO78165.1};
OS   Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO78165.1};
RN   [1] {ECO:0000313|EMBL:EDO78165.1, ECO:0000313|Proteomes:UP000001548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50803 / WB clone C6 {ECO:0000313|Proteomes:UP000001548},
RC   and WB C6 {ECO:0000313|EMBL:EDO78165.1};
RX   PubMed=17901334; DOI=10.1126/science.1143837;
RA   Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA   Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA   Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA   Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA   Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA   Svard S.G., Sogin M.L.;
RT   "Genomic minimalism in the early diverging intestinal parasite Giardia
RT   lamblia.";
RL   Science 317:1921-1926(2007).
RN   [2] {ECO:0000313|EMBL:KAE8304642.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB C6 {ECO:0000313|EMBL:KAE8304642.1};
RA   Xu F., Jex A., Svard S.G.;
RT   "New Giardia intestinalis WB genome in near-complete chromosomes.";
RL   Submitted (JUL-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDO78165.1}.
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DR   EMBL; AACB02000029; EDO78165.1; -; Genomic_DNA.
DR   EMBL; AACB03000001; KAE8304642.1; -; Genomic_DNA.
DR   RefSeq; XP_001705839.1; XM_001705787.1.
DR   AlphaFoldDB; A8BP13; -.
DR   STRING; 184922.A8BP13; -.
DR   EnsemblProtists; EDO78165; EDO78165; GL50803_16363.
DR   GeneID; 5698724; -.
DR   KEGG; gla:GL50803_0016363; -.
DR   VEuPathDB; GiardiaDB:GL50803_16363; -.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OMA; ESNEWAL; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001548; Chromosome 5.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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:EDO78165.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDO78165.1}.
FT   DOMAIN          98..461
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   479 AA;  53151 MW;  54CD52E4A74A9A00 CRC64;
     MPYQPVLTPE TCYKGLFDVK FSMVNLDLSS VEQKIAQKQA PFSSIIKCNL GNPQGVGQKP
     VTYLRQMVAG FACPDLIGKY VLPTDVELRV KHILNSCSGK SSGSYQATAG IPAVVDDVAA
     YISDRDEIPC NPATVCMANG ATEAIMTLLR PIIRNETDAI LCPRPGFPLY ASTIVYYGGK
     EVSYDLDESN EWALTQEALD AALQQCKDEG LTPRCLVLIN PNNPTGSTLT ESDIKNALRF
     AYKNDMMVMS DEVYQTNIYE PEEFPFLSAR KLLYALNAEG ECQGLELISI HSASKSIFGE
     CGRRGGYWQA ENLNPKFMEQ IMDIISLGST NTDGMMAMDV IVNPPRPGEP SYWKFKRECD
     ALYTSLQRKA RMVSHEMNSW RGLSCCKPSG AMYVFPRIHA PPAAIEAARL AGKEPDQLYC
     QDLLDSVGVF TLDGGMFGQK PGTYHLRMTI LPSEEVMTDL LARWKVFHEG WMSKYSAEE
//