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 16-JUN-2009, entry version 52. DE RecName: Full=Probable prephenate dehydrogenase [NADP+]; DE Short=PRDH; DE EC=1.3.1.13; GN ORFNames=SPCC1494.04c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., 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 MEDLINE=98162722; 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). CC -!- CATALYTIC ACTIVITY: Prephenate + NADP(+) = 4-hydroxyphenylpyruvate CC + CO(2) + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L- CC tyrosine from prephenate: step 1/2. CC -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; -. DR GeneID; 2539274; -. DR KEGG; spo:SPCC1494.04c; -. DR NMPDR; fig|4896.1.peg.867; -. DR GeneDB_Spombe; SPCC1494.04c; -. DR OMA; O60078; HVYAGLA. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-000428-MON; -. DR BRENDA; 1.3.1.13; 653. DR ArrayExpress; O60078; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IMP:GeneDB_SPombe. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP:GeneDB_SPombe. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003099; Prephen_DH. DR InterPro; IPR012385; Prephenate_DH_fun. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF02153; PDH; 1. DR PIRSF; PIRSF036510; PDH_fung; 1. DR PROSITE; PS51176; PDH_ADH; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Tyrosine biosynthesis. FT CHAIN 1 431 Probable prephenate dehydrogenase FT [NADP+]. FT /FTId=PRO_0000119207. FT DOMAIN 5 285 Prephenate/arogenate dehydrogenase. FT NP_BIND 5 34 NADP (Potential). FT CONFLICT 429 431 QKM -> KKCDFLIAAFCVYNS (in Ref. 2; FT BAA13874). 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 //