ID   A8BW60_GIAIC            Unreviewed;       521 AA.
AC   A8BW60;
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_0012150 {ECO:0000313|EMBL:KAE8302822.1},
GN   GL50803_12150 {ECO:0000313|EMBL:EDO76851.1};
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:EDO76851.1};
RN   [1] {ECO:0000313|EMBL:EDO76851.1, 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:EDO76851.1};
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:KAE8302822.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB C6 {ECO:0000313|EMBL:KAE8302822.1};
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:EDO76851.1}.
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DR   EMBL; AACB02000054; EDO76851.1; -; Genomic_DNA.
DR   EMBL; AACB03000003; KAE8302822.1; -; Genomic_DNA.
DR   RefSeq; XP_001704525.1; XM_001704473.1.
DR   AlphaFoldDB; A8BW60; -.
DR   SMR; A8BW60; -.
DR   STRING; 184922.A8BW60; -.
DR   EnsemblProtists; EDO76851; EDO76851; GL50803_12150.
DR   GeneID; 5697393; -.
DR   KEGG; gla:GL50803_0012150; -.
DR   VEuPathDB; GiardiaDB:GL50803_12150; -.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OMA; FGFECPP; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001548; Chromosome 3.
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:EDO76851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDO76851.1}.
FT   DOMAIN          111..473
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   521 AA;  58324 MW;  703D2EAEE04BC29B CRC64;
     MAPYNVFDLT TISQAVLQAE YAVRGTVPLR AIEIEDELKT PDGAKKYPFN RIIYSNIGNP
     MVMGLKYSTF LRNLLALVTA PHVLSKPDTE ICALLNCNQE CVDRARAFVK ENPSGVGAYT
     HSQGYLSVRK EVAAFIQQRD GFPSDPSNIY LSDGASVSVK TILQLLAGPN PGDGAFLLPI
     PQYPLYSAAI ALNNAVAVKY YLLEDDGWSI DLKSLREAIE THRKTAKSTI RALILVNPGN
     PSGSVFSRET LRAAIDICDE YGISIMSDEV YQLNTYAEAP GKQRPVFHSM KKVLCEWEKD
     KGRKGPALFS FHSVSKGLLG ECGLRGGYLE CYNVPKEITA QIYKCFSVCL CSNTIGQVVV
     SYMVNPPKSD DEDKKHLKTV FESMERKAQI LTEGLNKVPY MTCEVVSGAM YAFPRLYLPK
     RFVEEAEAGK MAADTLYCLK LLETTGVCGV PGNGFQQREN TFHMRITILE DEKFFHEFVE
     KISTFHKDLW KKYGSDSERA AYRKEIEERF ATMRKACHAE W
//