YI13_SCHPO
ID YI13_SCHPO Reviewed; 259 AA.
AC Q9P7B4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=NADP-dependent 3-hydroxy acid dehydrogenase {ECO:0000250|UniProtKB:Q05016};
DE AltName: Full=L-allo-threonine dehydrogenase {ECO:0000250|UniProtKB:Q05016};
DE EC=1.1.1.381 {ECO:0000250|UniProtKB:Q05016};
GN ORFNames=SPAC521.03;
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-43, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: NADP-dependent dehydrogenase with broad substrate specificity
CC acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-
CC allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously
CC decarboxylated into aminoacetone. Also acts on D-threonine, L-serine,
CC D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate
CC and L-glycerate. {ECO:0000250|UniProtKB:Q05016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH;
CC Xref=Rhea:RHEA:43524, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58320, ChEBI:CHEBI:58349, ChEBI:CHEBI:58585;
CC EC=1.1.1.381; Evidence={ECO:0000250|UniProtKB:Q05016};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q05016}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000250|UniProtKB:Q05016}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB86467.1; -; Genomic_DNA.
DR RefSeq; NP_593098.1; NM_001018495.2.
DR AlphaFoldDB; Q9P7B4; -.
DR SMR; Q9P7B4; -.
DR BioGRID; 279881; 10.
DR STRING; 4896.SPAC521.03.1; -.
DR iPTMnet; Q9P7B4; -.
DR MaxQB; Q9P7B4; -.
DR PaxDb; Q9P7B4; -.
DR PRIDE; Q9P7B4; -.
DR EnsemblFungi; SPAC521.03.1; SPAC521.03.1:pep; SPAC521.03.
DR GeneID; 2543461; -.
DR KEGG; spo:SPAC521.03; -.
DR PomBase; SPAC521.03; -.
DR VEuPathDB; FungiDB:SPAC521.03; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; Q9P7B4; -.
DR OMA; WRWMWET; -.
DR PhylomeDB; Q9P7B4; -.
DR PRO; PR:Q9P7B4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..259
FT /note="NADP-dependent 3-hydroxy acid dehydrogenase"
FT /id="PRO_0000372617"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 39..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 65..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 188..195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 259 AA; 28149 MW; EA8FBCBF231FCC08 CRC64;
MSRLDGKTIL ITGASSGIGK STAFEIAKVA KVKLILAARR FSTVEEIAKE LESKYEVSVL
PLKLDVSDLK SIPGVIESLP KEFADIDVLI NNAGLALGTD KVIDLNIDDA VTMITTNVLG
MMAMTRAVLP IFYSKNKGDI LNVGSIAGRE SYVGGSVYCS TKSALAQFTS ALRKETIDTR
IRIMEVDPGL VETEFSVVRF HGDKQKADNV YKNSEPLTPE DIAEVILFAL TRRENVVIAD
TLVFPSHQGG ANHVYRKQA
