ID C4XXQ1_CLAL4 Unreviewed; 560 AA.
AC C4XXQ1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=CLUG_00723 {ECO:0000313|EMBL:EEQ36600.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36600.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ36600.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36600.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408076; EEQ36600.1; -; Genomic_DNA.
DR RefSeq; XP_002619564.1; XM_002619518.1.
DR AlphaFoldDB; C4XXQ1; -.
DR STRING; 306902.C4XXQ1; -.
DR GeneID; 8500416; -.
DR KEGG; clu:CLUG_00723; -.
DR VEuPathDB; FungiDB:CLUG_00723; -.
DR HOGENOM; CLU_014254_3_0_1; -.
DR InParanoid; C4XXQ1; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000007703; Unassembled WGS sequence.
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:UP000007703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..536
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 560 AA; 62649 MW; 029BADAE1E452007 CRC64;
MIVAPHMSVH PFSPLFFKTR AYFSAGRHVS YLKVNRVIEK KKFRLLSIMS SLRLSSRSLL
LKRLYASFKP APQLTVSDLN ESTLEAKYAV RGKIPIRADE LRSEIDSNPD GHGLPYDRII
SANIGNPQQL DQQPLSWYRQ VLSLMQYPTL INKISTLDKK TADSLYPPDV VERARKLLKT
TGSVGAYSHS QGDITVRKSV AKFISERDGY AAHPQNIFLT SGASSAVSYL IQVLSSSPNA
GFLIPIPQYP LYTASIALNN AKPIGYFLDE DSHWSTDPVQ IRRLIDENKA NGVDLKALVV
INPGNPTGAI LTEKDIAEII DIAAEHGLVL IADEVYQENV FEGKFVSMKK VYAQLLEKDP
ETYKHVQLAS LHSTSKGVSG ECGQRGGYME LVGFSQEVRD IIFKLASINL CPVVSGQALV
ELMINPPKEG EPSYELYQKE TTGIHDDLMK RASLLYKSFC AMTDVQCNKP QGAMYLFPSL
KFTKETYSKL FEASEELNLT PDEYYCTELL EKTGICCVPG NGFGQVPGTY HLRTTFLPPG
TKWIEEWTKF HEDFVSKYKN
//
