ID GLY1_YEAST Reviewed; 387 AA.
AC P37303; D3DLK4; P32615;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Low specificity L-threonine aldolase;
DE Short=Low specificity L-TA;
DE Short=TA;
DE EC=4.1.2.48;
GN Name=GLY1; OrderedLocusNames=YEL046C; ORFNames=SYGP-ORF34;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=8132653; DOI=10.1016/s0021-9258(17)37089-8;
RA McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F.-R., Tang S., Bognar A.L.;
RT "Cloning and molecular characterization of three genes, including two genes
RT encoding serine hydroxymethyltransferases, whose inactivation is required
RT to render yeast auxotrophic for glycine.";
RL J. Biol. Chem. 269:9155-9165(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=9151955; DOI=10.1111/j.1432-1033.1997.00289.x;
RA Liu J.-Q., Nagata S., Dairi T., Misono H., Shimizu S., Yamada H.;
RT "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-
RT threonine aldolase that catalyzes cleavage of L-allo-threonine and L-
RT threonine to glycine -- expression of the gene in Escherichia coli and
RT purification and characterization of the enzyme.";
RL Eur. J. Biochem. 245:289-293(1997).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9163906; DOI=10.1111/j.1574-6968.1997.tb10349.x;
RA Monschau N., Stahmann K.-P., Sahm H., McNeil J.B., Bognar A.L.;
RT "Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a
RT key enzyme in glycine biosynthesis.";
RL FEMS Microbiol. Lett. 150:55-60(1997).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-369 AND THR-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC glycine and acetaldehyde.
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 Evidence={ECO:0000269|PubMed:9151955};
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 Evidence={ECO:0000269|PubMed:9151955};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC allo-threonine: step 1/1.
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via aldolase
CC pathway; acetaldehyde and glycine from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- MISCELLANEOUS: Present with 106000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR EMBL; L28739; AAA72430.1; -; Genomic_DNA.
DR EMBL; U18779; AAB64996.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07608.1; -; Genomic_DNA.
DR PIR; S30831; S30831.
DR RefSeq; NP_010868.1; NM_001178861.1.
DR AlphaFoldDB; P37303; -.
DR SMR; P37303; -.
DR BioGRID; 36684; 60.
DR DIP; DIP-4287N; -.
DR IntAct; P37303; 6.
DR STRING; 4932.YEL046C; -.
DR iPTMnet; P37303; -.
DR MaxQB; P37303; -.
DR PaxDb; 4932-YEL046C; -.
DR PeptideAtlas; P37303; -.
DR EnsemblFungi; YEL046C_mRNA; YEL046C; YEL046C.
DR GeneID; 856665; -.
DR KEGG; sce:YEL046C; -.
DR AGR; SGD:S000000772; -.
DR SGD; S000000772; GLY1.
DR VEuPathDB; FungiDB:YEL046C; -.
DR eggNOG; KOG1368; Eukaryota.
DR GeneTree; ENSGT00390000014681; -.
DR HOGENOM; CLU_029381_1_0_1; -.
DR InParanoid; P37303; -.
DR OMA; LVRIKAW; -.
DR OrthoDB; 178754at2759; -.
DR BioCyc; MetaCyc:YEL046C-MONOMER; -.
DR BioCyc; YEAST:YEL046C-MONOMER; -.
DR BRENDA; 4.1.2.48; 984.
DR SABIO-RK; P37303; -.
DR UniPathway; UPA00044; UER00429.
DR UniPathway; UPA00288; UER00427.
DR BioGRID-ORCS; 856665; 10 hits in 10 CRISPR screens.
DR PRO; PR:P37303; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P37303; Protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IDA:SGD.
DR GO; GO:0004793; F:threonine aldolase activity; IDA:SGD.
DR GO; GO:0006545; P:glycine biosynthetic process; IDA:SGD.
DR GO; GO:0006567; P:threonine catabolic process; IDA:SGD.
DR CDD; cd06502; TA_like; 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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Lyase; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..387
FT /note="Low specificity L-threonine aldolase"
FT /id="PRO_0000121572"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 253
FT /note="M -> I (in Ref. 1; AAA72430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42815 MW; 46139EB459442852 CRC64;
MTEFELPPKY ITAANDLRSD TFTTPTAEMM EAALEASIGD AVYGEDVDTV RLEQTVARMA
GKEAGLFCVS GTLSNQIAIR THLMQPPYSI LCDYRAHVYT HEAAGLAILS QAMVVPVVPS
NGDYLTLEDI KSHYVPDDGD IHGAPTRLIS LENTLHGIVY PLEELVRIKA WCMENGLKLH
CDGARIWNAA AQSGVPLKQY GEIFDSISIC LSKSMGAPIG SVLVGNLKFV KKATHFRKQQ
GGGIRQSGMM ARMALVNINN DWKSQLLYSH SLAHELAEYC EAKGIPLESP ADTNFVFINL
KAARMDPDVL VKKGLKYNVK LMGGRVSFHY QVTRDTLEKV KLAISEAFDY AKEHPFDCNG
PTQIYRSEST EVDVDGNAIR EIKTYKY
//
