ID   Q6CJE9_KLULA            Unreviewed;       528 AA.
AC   Q6CJE9;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=KLLA0_F19162g {ECO:0000313|EMBL:CAG98648.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG98648.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAG98648.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382126; CAG98648.1; -; Genomic_DNA.
DR   RefSeq; XP_455940.1; XM_455940.1.
DR   AlphaFoldDB; Q6CJE9; -.
DR   STRING; 284590.Q6CJE9; -.
DR   PaxDb; 284590-Q6CJE9; -.
DR   GeneID; 2895534; -.
DR   KEGG; kla:KLLA0_F19162g; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; Q6CJE9; -.
DR   OMA; FGFECPP; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000000598; Chromosome F.
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:UP000000598};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          140..506
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   528 AA;  59074 MW;  5E46A89C84F71FB7 CRC64;
     MLSVRVNLKT RISSGMIRVN APALKSTMPS VTSLTQLRFS TTVKPAPKLS LDDVNENVLK
     AKYAVRGRIP MRAEELRDQL KKDPSSLPFS KIISANIGNP QQLDQKPLTF YREVLSLLQH
     PELLEEADEA LQTLYKTDSI KRAKRLLSEV GGSVGAYSQS QGVQGIRETV ADFITKRDDG
     EISYPEDIYL TAGASAAVSY ILSILCKGPN TGVLIPIPQY PLYTASLALN NSRPLPYYLR
     EEQNWSTDPE EIEQVVLDAI QKGIKPTCLV VINPGNPTGA ILSEQSIQKI FEVAAKYGIV
     VIADEVYQEN VFKGSKFYSM KKVLRNLQKT YHGQYDNIQL ASLHSTSKGV SGECGQRGGY
     MELVGFNHDI RQVFLKLASI SLCPVVTGQA LVDLMVSPPQ PGDESYEQDQ QEREDIHDAL
     DERASKLFET FSRLEGIECR KPQGAMYLYP KLDLPYKVIQ EAQHLEMEPD EFYCKALLEN
     TGICTVPGSG FGQVPGTYHL RTTFLPPGTE WVETWEKFHK AFFDKYRD
//