ID   B7FUH0_PHATC            Unreviewed;       475 AA.
AC   B7FUH0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, 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=PHATRDRAFT_34010 {ECO:0000313|EMBL:EEC50258.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC50258.1, ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC50258.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC50258.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA   Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) 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; CM000607; EEC50258.1; -; Genomic_DNA.
DR   RefSeq; XP_002178593.1; XM_002178557.1.
DR   AlphaFoldDB; B7FUH0; -.
DR   STRING; 556484.B7FUH0; -.
DR   PaxDb; 2850-Phatr34010; -.
DR   GeneID; 7197795; -.
DR   KEGG; pti:PHATRDRAFT_34010; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; B7FUH0; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000000759; Chromosome 4.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; 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   Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          92..463
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   475 AA;  51937 MW;  578A301D8C2712AD CRC64;
     MYPGLRKMEY AVRGKVVIAA DQISDNLASG KSYPFDHIVY TNIGNPQSVG QQPLTWPRQV
     LALVDLPDAV GIQHPDILRL FPADAVARAK EIKEGLGGHG SGAYSHSKGC RAFRRDIAAF
     LQDRDGGLPA EPEDIFMTNG ASAGINMMLN ALVADSSCGV MIPIPQYPIY SATIDLLGGQ
     KVGYYLNEAN GWELNMEELE RSLQEATEQG IKVNAFVLIN PGNPSGTVLS RTNLQDIVRF
     CAKHNLVLLA DEVYQENVYD ENAEFVSCKR AAHQVGLLED DGIELVSFHS ISKGVFGECG
     RRGGYMELVG FNADVKDELY KLASANLCAT VSGQIMTSLM VRGPDQGDVS YESHQAEKKA
     IFESLRRRSK IVSDGLNNIP GISCQTATGS MYCFPSVEMP KGALPAAEKM GVSPDTLYCM
     SLLERTGLCV VPASGFGQRE GRYGFRTTFL PSEDEMARAV EQIREHYHEF CEMYA
//