GLY1_SCHPO
ID GLY1_SCHPO Reviewed; 376 AA.
AC O13940;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable low-specificity L-threonine aldolase;
DE EC=4.1.2.48;
GN Name=gly1; ORFNames=SPAC23H3.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB16235.1; -; Genomic_DNA.
DR PIR; T38302; T38302.
DR RefSeq; NP_593799.1; NM_001019228.2.
DR AlphaFoldDB; O13940; -.
DR SMR; O13940; -.
DR BioGRID; 278343; 11.
DR STRING; 4896.SPAC23H3.09c.1; -.
DR iPTMnet; O13940; -.
DR MaxQB; O13940; -.
DR PaxDb; O13940; -.
DR PRIDE; O13940; -.
DR EnsemblFungi; SPAC23H3.09c.1; SPAC23H3.09c.1:pep; SPAC23H3.09c.
DR GeneID; 2541852; -.
DR KEGG; spo:SPAC23H3.09c; -.
DR PomBase; SPAC23H3.09c; gly1.
DR VEuPathDB; FungiDB:SPAC23H3.09c; -.
DR eggNOG; KOG1368; Eukaryota.
DR HOGENOM; CLU_029381_1_1_1; -.
DR InParanoid; O13940; -.
DR OMA; NKGGGAC; -.
DR PhylomeDB; O13940; -.
DR UniPathway; UPA00044; UER00429.
DR PRO; PR:O13940; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; ISS:PomBase.
DR GO; GO:0006567; P:threonine catabolic process; ISS:PomBase.
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; Reference proteome.
FT CHAIN 1..376
FT /note="Probable low-specificity L-threonine aldolase"
FT /id="PRO_0000121571"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41318 MW; FBB8FB5C2F402D1D CRC64;
MSGSVTSTTT ETRLCPSNQG SAKKYRPWND FRSDTLTVPT DEMRRIMYEA SDGDCVYEED
EDTRKLEVYV AKLTGKEAAL FVTSGTQGNQ LCIRSHLHQP PHSIICDDRA HIYNWEAGAI
GLFTQAIVRP ISPKNNVYIT AEEIENKLIL GNDIHFSPTG LICLENTIKG AVVPLDEVAR
ISGLAKAHKI PLHCDGARLW DAAVASNVSI KEYCSYFDSV SLCLSKGLAA PVGSIIVGPR
DFIAKAKWFR KAYGGGLRQS GMLAAAGLYS IQHNFPLLKQ VHKYAIEVAE YAESLGIELE
VPTQSNMVTL ANINVAILCD EAKKSGIILM GPRIVFHIQI TPDAVEILKN VLRRTVERQA
VETHIVAKPG EFCVGY
