PUT2_SCHPO
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 25-MAY-2022, entry version 140.
DE RecName: Full=Probable delta-1-pyrroline-5-carboxylate dehydrogenase;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN ORFNames=SPBC24C6.04;
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 189-548.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-394 AND SER-396, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
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 {ECO:0000305}.
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DR EMBL; CU329671; CAA21148.1; -; Genomic_DNA.
DR EMBL; D89230; BAA13891.1; -; mRNA.
DR PIR; T39968; T39968.
DR RefSeq; NP_595958.1; NM_001021867.2.
DR AlphaFoldDB; O74766; -.
DR SMR; O74766; -.
DR BioGRID; 276915; 21.
DR STRING; 4896.SPBC24C6.04.1; -.
DR iPTMnet; O74766; -.
DR MaxQB; O74766; -.
DR PaxDb; O74766; -.
DR PRIDE; O74766; -.
DR EnsemblFungi; SPBC24C6.04.1; SPBC24C6.04.1:pep; SPBC24C6.04.
DR PomBase; SPBC24C6.04; -.
DR VEuPathDB; FungiDB:SPBC24C6.04; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; O74766; -.
DR OMA; FAGIHFT; -.
DR PhylomeDB; O74766; -.
DR UniPathway; UPA00261; UER00374.
DR PRO; PR:O74766; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; ISS:PomBase.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; ISO:PomBase.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005931; P5CDH/ALDH4A1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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 NAD; Oxidoreductase; Phosphoprotein; Proline metabolism;
KW Reference proteome.
FT CHAIN 1..548
FT /note="Probable delta-1-pyrroline-5-carboxylate
FT dehydrogenase"
FT /id="PRO_0000056502"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT SITE 193
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 210
FT /note="N -> K (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> F (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..274
FT /note="FR -> IC (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="K -> N (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="E -> G (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="K -> E (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="F -> Y (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="S -> Y (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="F -> L (in Ref. 2; BAA13891)"
FT /evidence="ECO:0000305"
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
