ID PUT2_SCHPO Reviewed; 548 AA. AC O74766; P78880; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Probable delta-1-pyrroline-5-carboxylate dehydrogenase; DE Short=P5C dehydrogenase; DE EC=1.5.1.12; GN ORFNames=SPBC24C6.04; 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 189-548. 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). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-394 AND RP SER-396, AND 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 -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 CC H(2)O = L-glutamate + NAD(P)H. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 2/2. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. 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; CU329671; CAA21148.1; -; Genomic_DNA. DR EMBL; D89230; BAA13891.1; -; mRNA. DR PIR; T39968; T39968. DR RefSeq; NP_595958.1; -. DR GeneID; 2540387; -. DR KEGG; spo:SPBC24C6.04; -. DR NMPDR; fig|4896.1.peg.1824; -. DR GeneDB_Spombe; SPBC24C6.04; -. DR OMA; O74766; RYAAGNY. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-004021-MON; -. DR BRENDA; 1.5.1.12; 653. DR ArrayExpress; O74766; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0005759; C:mitochondrial matrix; IEA:InterPro. DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR005931; d-1-pyrroline-5-COlate_DH-1. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Phosphoprotein; KW Proline metabolism. FT CHAIN 1 548 Probable delta-1-pyrroline-5-carboxylate FT dehydrogenase. FT /FTId=PRO_0000056502. FT ACT_SITE 298 298 Proton acceptor (By similarity). FT ACT_SITE 332 332 Nucleophile (By similarity). FT SITE 193 193 Transition state stabilizer (By FT similarity). FT MOD_RES 391 391 Phosphoserine. FT MOD_RES 394 394 Phosphoserine. FT MOD_RES 396 396 Phosphoserine. FT CONFLICT 210 210 N -> K (in Ref. 2; BAA13891). FT CONFLICT 264 264 L -> F (in Ref. 2; BAA13891). FT CONFLICT 273 274 FR -> IC (in Ref. 2; BAA13891). FT CONFLICT 294 294 K -> N (in Ref. 2; BAA13891). FT CONFLICT 502 502 E -> G (in Ref. 2; BAA13891). FT CONFLICT 516 516 K -> E (in Ref. 2; BAA13891). FT CONFLICT 526 526 F -> Y (in Ref. 2; BAA13891). FT CONFLICT 531 531 S -> Y (in Ref. 2; BAA13891). FT CONFLICT 536 536 F -> L (in Ref. 2; BAA13891). SQ SEQUENCE 548 AA; 60219 MW; E14D37E32A0B4B6E CRC64; MSQFAEFKLP AIKNEPPKHY GPNSADREGI VKAYKELEAE LPVTIPVIID GKEVETNTIG EQRCPFEHKK VVARYHRAGA KHVEDAIEAA LRGKKVWESL PFADRSAIFL KAAHLISTKY RYKLMAATMI GQGKNIWQAE IDAGMEIIDF LRFNTKYASE LYASQPPENT PGVWNRMEYR PLEGFVYAIT PFNFTAIAGN LAAAPLLMGN VVLMKPSDHA VLSSYIVYQI FREAGLPAGA LQFIPGDAVE VSKVCFNHPE FAGLHFTGST AVFRSLWGTI GENVANGKYR TYPKIVGETG GKNFHLVHSS AEIKSAVVNA VRAAFEYQGQ KCSALSRLYV SKYAWENGFR DELTKQVKSL KVGAPLTDFA NFVGPVIHQA SFNKLKKVLE SAASDSEIEV LAGGKADDSE GFFVEPTVLL SKNPKHDIFV NELFGPVLSV YVYEDDNLDA VCDLIDTTTP YGLTGSIFAQ DRVVVRKLTD RLRNAAGNFY INDKCTGAVV GEQPFGGARA SGTNDKAGSG MILSRFVSPR SIKDTFAYAD SVLYPSNF //