ID H2AR48_KAZAF Unreviewed; 514 AA.
AC H2AR48;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN Name=KAFR0B05530 {ECO:0000313|EMBL:CCF56848.1};
GN ORFNames=KAFR_0B05530 {ECO:0000313|EMBL:CCF56848.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF56848.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF56848.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650822; CCF56848.1; -; Genomic_DNA.
DR RefSeq; XP_003955983.1; XM_003955934.1.
DR AlphaFoldDB; H2AR48; -.
DR STRING; 1071382.H2AR48; -.
DR GeneID; 13884730; -.
DR KEGG; kaf:KAFR_0B05530; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; H2AR48; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000005220; Chromosome 2.
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; AT04676P; 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:UP000005220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 133..494
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 514 AA; 57405 MW; D099A04495D1382F CRC64;
MQLTEEFAAT TQYFPVRKAL DDDTIHNFKP AKKITLDDLN QNVLKSEYAV RGSIPRRAEE
LEFELLNNDS SDSLAFENIV HANIGNPQQL DQKPLTFSRQ VISILQYPEL LNQRNILVST
GIFKSDAMER AETLLCHIGG SVGAYSSSQG VYGIRETVAN YITARDNGET ASPDDIFLTE
GASKAASYLL SLLCKDKNTG VLIPIPQYPL YTATITLCDA KMLPYYLNEE SGWSTNTNEI
EKVVLDAIAD NVKPSVMVVI NPGNPTGSVL SKDDIIHIIN IGAKYGIVLI ADEVYQENIF
DGEFHSMKKV LRSLQKQYPG KYDAVQLASL HSTSKGVSGE CGQRGGYMEL VGFKDEIRQA
ILKLASISLC SVITGQALVD LMVNPPKKGD ESYELDNFER KNIHETLKER AEKLYNLFCQ
LKGVECQKPQ GAMYLFPKLH FPQTLITEAI NQNMSPDEFY CHALLEATGI CTVPGSGFGQ
KEGTYHLRTT FLAPGNQWTE KWKLFHEEFF SKYQ
//