ID   GLY1_CANAX              Reviewed;         374 AA.
AC   O13427;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Low-specificity L-threonine aldolase;
DE            EC=4.1.2.48;
GN   Name=GLY1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10641038;
RX   DOI=10.1002/(sici)1097-0061(20000130)16:2<167::aid-yea519>3.0.co;2-1;
RA   McNeil J.B., Flynn J., Tsao N., Monschau N., Stahmann K., Haynes R.H.,
RA   McIntosh E.M., Pearlman R.E.;
RT   "Glycine metabolism in Candida albicans: characterization of the serine
RT   hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1)
RT   genes.";
RL   Yeast 16:167-175(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-allo-threonine = acetaldehyde + glycine;
CC         Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:58585; EC=4.1.2.48;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via aldolase
CC       pathway; acetaldehyde and glycine from L-threonine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR   EMBL; AF009967; AAB64198.1; -; Genomic_DNA.
DR   AlphaFoldDB; O13427; -.
DR   SMR; O13427; -.
DR   VEuPathDB; FungiDB:C1_10450W_A; -.
DR   VEuPathDB; FungiDB:CAWG_00388; -.
DR   BRENDA; 4.1.2.48; 1096.
DR   UniPathway; UPA00044; UER00429.
DR   GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR48097:SF9; PTHR48097:SF9; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..374
FT                   /note="Low-specificity L-threonine aldolase"
FT                   /id="PRO_0000121570"
FT   REGION          354..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  41811 MW;  AE44C349FA83F7C0 CRC64;
     MTADEEETFT TFNEFRSDTF TVPTRAMVED GFMNATFGDS VYQEDETTLR LESKMCEITG
     KPAALFCVSG TMSNQIGLRA NLVQPPYSIL CDYRAHVFLH EAGGLATLSQ AMVHPVRPSN
     GNYLTFEDVL GNVTYDDDGD IHAAPTKVIS LENTLHGIII PIEEIRKISE FCRENDIRLH
     LDGARLWNAS VATGISIKEY CSYFDSVSLC LSKSLGAPIG SVLVGDEKFI RKANHFKKQS
     GGGIRQAGIM SAMAIHAIDY NLSKLELSHN YAKQIGDFCQ EHGIKLESPV DTSLVFLDLK
     ANKMDPNRLV ELGRTKYNVK LMGQRIACHF QLSQESVDNV KKCILECLEY HQKHPHKDDG
     RNNKKMYSLD AIKK