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UniProtKB/Swiss-Prot entry O74766


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PUT2_SCHPO
Primary accession number O74766
Secondary accession number P78880
Integrated into Swiss-Prot on May 16, 2003
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Probable delta-1-pyrroline-5-carboxylate dehydrogenase
Synonyms P5C dehydrogenase
EC 1.5.1.12
Gene name
ORFNames: SPBC24C6.04
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-548.
STRAIN=PR745;
DOI=10.1093/dnares/4.6.363; PubMed=9501991 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe cDNAs.";
DNA Res. 4:363-369(1997).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-394 AND SER-396, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329671; CAA21148.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D89230; BAA13891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39968; T39968.
RefSeq NP_595958.1; -.
3D structure databases
ModBase O74766.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004021-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC24C6.04; -.
Gene expression databases
ArrayExpress O74766; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from InterPro).
GO:0003842; Molecular function: 1-pyrroline-5-carboxylate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561; Biological process: proline biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005931; d-1-pyrroline-5-COlate_DHase-1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01236; D1pyr5carbox1; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
Genome annotation databases
GeneID 2540387; -.
KEGG spo:SPBC24C6.04; -.
NMPDR fig|4896.1.peg.1824; -.
Other
ProtoNet O74766.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase; Phosphoprotein; Proline metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   548  548     Probable delta-1-pyrroline-5-carboxylate dehydrogenase. PRO_0000056502
ACT_SITE   298   298        Proton acceptor (By similarity). 
ACT_SITE   332   332        Nucleophile (By similarity). 
SITE   193   193  1     Transition state stabilizer (By similarity). 
MOD_RES   391   391        Phosphoserine. 
MOD_RES   394   394        Phosphoserine. 
MOD_RES   396   396        Phosphoserine. 
CONFLICT   210   210        N -> K (in Ref. 2; BAA13891). 
CONFLICT   264   264        L -> F (in Ref. 2; BAA13891). 
CONFLICT   273   274        FR -> IC (in Ref. 2; BAA13891). 
CONFLICT   294   294        K -> N (in Ref. 2; BAA13891). 
CONFLICT   502   502        E -> G (in Ref. 2; BAA13891). 
CONFLICT   516   516        K -> E (in Ref. 2; BAA13891). 
CONFLICT   526   526        F -> Y (in Ref. 2; BAA13891). 
CONFLICT   531   531        S -> Y (in Ref. 2; BAA13891). 
CONFLICT   536   536        F -> L (in Ref. 2; BAA13891). 
Sequence information
Length: 548 AA [This is the length of the unprocessed precursor] Molecular weight: 60219 Da [This is the MW of the unprocessed precursor] CRC64: E14D37E32A0B4B6E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQFAEFKLP AIKNEPPKHY GPNSADREGI VKAYKELEAE LPVTIPVIID GKEVETNTIG 

        70         80         90        100        110        120 
EQRCPFEHKK VVARYHRAGA KHVEDAIEAA LRGKKVWESL PFADRSAIFL KAAHLISTKY 

       130        140        150        160        170        180 
RYKLMAATMI GQGKNIWQAE IDAGMEIIDF LRFNTKYASE LYASQPPENT PGVWNRMEYR 

       190        200        210        220        230        240 
PLEGFVYAIT PFNFTAIAGN LAAAPLLMGN VVLMKPSDHA VLSSYIVYQI FREAGLPAGA 

       250        260        270        280        290        300 
LQFIPGDAVE VSKVCFNHPE FAGLHFTGST AVFRSLWGTI GENVANGKYR TYPKIVGETG 

       310        320        330        340        350        360 
GKNFHLVHSS AEIKSAVVNA VRAAFEYQGQ KCSALSRLYV SKYAWENGFR DELTKQVKSL 

       370        380        390        400        410        420 
KVGAPLTDFA NFVGPVIHQA SFNKLKKVLE SAASDSEIEV LAGGKADDSE GFFVEPTVLL 

       430        440        450        460        470        480 
SKNPKHDIFV NELFGPVLSV YVYEDDNLDA VCDLIDTTTP YGLTGSIFAQ DRVVVRKLTD 

       490        500        510        520        530        540 
RLRNAAGNFY INDKCTGAVV GEQPFGGARA SGTNDKAGSG MILSRFVSPR SIKDTFAYAD 


SVLYPSNF 

O74766 in FASTA format

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