TYR1_SCHPO
ID TYR1_SCHPO Reviewed; 431 AA.
AC O60078; P78863;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable prephenate dehydrogenase [NADP(+)];
DE Short=PRDH;
DE EC=1.3.1.13;
GN Name=tyr1; ORFNames=SPCC1494.04c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-431.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA19302.1; -; Genomic_DNA.
DR EMBL; D89213; BAA13874.1; -; mRNA.
DR PIR; T41005; T41005.
DR PIR; T43017; T43017.
DR RefSeq; NP_588529.1; NM_001023517.2.
DR AlphaFoldDB; O60078; -.
DR SMR; O60078; -.
DR STRING; 4896.SPCC1494.04c.1; -.
DR MaxQB; O60078; -.
DR PaxDb; O60078; -.
DR EnsemblFungi; SPCC1494.04c.1; SPCC1494.04c.1:pep; SPCC1494.04c.
DR GeneID; 2539274; -.
DR KEGG; spo:SPCC1494.04c; -.
DR PomBase; SPCC1494.04c; tyr1.
DR VEuPathDB; FungiDB:SPCC1494.04c; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; O60078; -.
DR OMA; WWKLGIV; -.
DR PhylomeDB; O60078; -.
DR UniPathway; UPA00122; UER00962.
DR PRO; PR:O60078; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IMP:PomBase.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP:PomBase.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR012385; Prephenate_DH_fun.
DR Pfam; PF02153; PDH; 1.
DR PIRSF; PIRSF036510; PDH_fung; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..431
FT /note="Probable prephenate dehydrogenase [NADP(+)]"
FT /id="PRO_0000119207"
FT DOMAIN 5..285
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT BINDING 5..34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 429..431
FT /note="QKM -> KKCDFLIAAFCVYNS (in Ref. 2; BAA13874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48906 MW; C598458426E620D7 CRC64;
MKETFQVGII GFGDMGRLYA EYISKAGWRV NVCDRPENYE SIQATYGNGG YTVLKDGFQV
SRTSDYILYS VEAEHIDKVV ALYGPATKVG AIVGGQTSCK APEMNAFEKY LPEDVDIISC
HSMHGPKVNP KSQPLVIIRH RASDEHFEIV NEILSCFKSS VVYLSAKEHD RITADTQAVT
HAAFLTMGLA WHANNQYPWE INRWCGGIEN IKMNLSMRIY SSKWHVYAGL AILNPEAQRQ
IQQYASSVTE LFKLAISGKA KEYEDRIRNA GKFVFGENMD RNSSGLLLSD ELLDQYSISN
IPKDESKRNS HLSILAIVDS WSKLGIHPQN HMICSTPLFR LWVGVSEYVF RHPGLLDSCI
YTATKHNDFS PDDLEFVVAV RSWSECVAAK DFTTYKKRFL ETQEYFRPRF EEATRVGNAM
ISKLLENLQK M
