ID   GLY1_ASHGO              Reviewed;         382 AA.
AC   O74267; Q753E8;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Low-specificity L-threonine aldolase;
DE            EC=4.1.2.48;
GN   Name=GLY1; OrderedLocusNames=AFR366W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=9797278; DOI=10.1128/aem.64.11.4283-4290.1998;
RA   Monschau N., Sahm H., Stahmann K.-P.;
RT   "Threonine aldolase overexpression plus threonine supplementation enhanced
RT   riboflavin production in Ashbya gossypii.";
RL   Appl. Environ. Microbiol. 64:4283-4290(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 14.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AJ005442; CAA06545.1; -; Genomic_DNA.
DR   EMBL; AE016819; AAS53737.2; -; Genomic_DNA.
DR   RefSeq; NP_985913.2; NM_211268.2.
DR   AlphaFoldDB; O74267; -.
DR   SMR; O74267; -.
DR   STRING; 33169.AAS53737; -.
DR   EnsemblFungi; AAS53737; AAS53737; AGOS_AFR366W.
DR   GeneID; 4622183; -.
DR   KEGG; ago:AGOS_AFR366W; -.
DR   eggNOG; KOG1368; Eukaryota.
DR   HOGENOM; CLU_029381_1_1_1; -.
DR   InParanoid; O74267; -.
DR   OMA; RISAWAK; -.
DR   UniPathway; UPA00044; UER00429.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central.
DR   GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; Reference proteome.
FT   CHAIN           1..382
FT                   /note="Low-specificity L-threonine aldolase"
FT                   /id="PRO_0000121569"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  42600 MW;  C3EC74B73AE8E947 CRC64;
     MNQDMELPEA YTSASNDFRS DTFTTPTREM IEAALTATIG DAVYQEDIDT LKLEQHVAKL
     AGMEAGMFCV SGTLSNQIAL RTHLTQPPYS ILCDYRAHVY THEAAGLAIL SQAMVTPVIP
     SNGNYLTLED IKKHYIPDDG DIHGAPTKVI SLENTLHGII HPLEELVRIK AWCMENDLRL
     HCDGARIWNA SAESGVPLKQ YGELFDSISI CLSKSMGAPM GSILVGSHKF IKKANHFRKQ
     QGGGVRQSGM MCKMAMVAIQ GDWKGKMRRS HRMAHELARF CAEHGIPLES PADTNFVFLD
     LQKSKMNPDV LVKKSLKYGC KLMGGRVSFH YQISEESLEK IKQAILEAFE YSKKNPYDEN
     GPTKIYRSES ADAVGEIKTY KY