PROA_SCHPO
ID PROA_SCHPO Reviewed; 451 AA.
AC Q9UT44;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Probable gamma-glutamyl phosphate reductase;
DE Short=GPR;
DE EC=1.2.1.41;
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE Short=GSA dehydrogenase;
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
GN Name=pro1; ORFNames=SPAC821.11;
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).
CC -!- FUNCTION: Catalyzes the NADPH dependent reduction of L-gamma-glutamyl
CC 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB57445.1; -; Genomic_DNA.
DR PIR; T41722; T41722.
DR RefSeq; NP_593164.1; NM_001018562.2.
DR AlphaFoldDB; Q9UT44; -.
DR SMR; Q9UT44; -.
DR BioGRID; 279832; 4.
DR STRING; 4896.SPAC821.11.1; -.
DR iPTMnet; Q9UT44; -.
DR MaxQB; Q9UT44; -.
DR PaxDb; Q9UT44; -.
DR PRIDE; Q9UT44; -.
DR EnsemblFungi; SPAC821.11.1; SPAC821.11.1:pep; SPAC821.11.
DR GeneID; 2543410; -.
DR KEGG; spo:SPAC821.11; -.
DR PomBase; SPAC821.11; pro1.
DR VEuPathDB; FungiDB:SPAC821.11; -.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_030231_0_1_1; -.
DR InParanoid; Q9UT44; -.
DR OMA; PGVCNAM; -.
DR PhylomeDB; Q9UT44; -.
DR Reactome; R-SPO-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00360.
DR PRO; PR:Q9UT44; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; ISO:PomBase.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006561; P:proline biosynthetic process; EXP:PomBase.
DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00412; ProA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR020593; G-glutamylP_reductase_CS.
DR InterPro; IPR012134; Glu-5-SA_DH.
DR InterPro; IPR000965; GPR_dom.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF000151; GPR; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
DR PROSITE; PS01223; PROA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; NADP; Oxidoreductase; Proline biosynthesis;
KW Reference proteome.
FT CHAIN 1..451
FT /note="Probable gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189823"
SQ SEQUENCE 451 AA; 48707 MW; 9F823DD58A2B46E0 CRC64;
MSLEENVKEA KNAFNILQTL SVEDRDDALD KIVEELRIKK SEVLAANAED MKAAKLLAES
GKLSSSMVKR LDLSSSDKYD SMVQGVLDVK SLPDPLGRVT YARSLDDGLD LYKVSCPVGL
LLVIFEARPE VIINITSLAI KSGNAVVLKG GTESAKSFAA LSNVVRSALG KSKVPQAAVQ
LVQSREEVSQ LLKLDEYIDL VIPRGSTNLV RHIKDNTKIP VLGHAAGLCS MYVHEDADME
LASKLVLDGK TDYPAACNAI ETLLINEAVL SSHLPKIAET LTEAKVTLKC DPASLKVLKD
MPKVSALVEP SVDQDYNTEF SDLILAIKTV PSLQSAMQHI NTHGSKHTDC IITSSEAAAN
RFMAGIDASG VYWNASTRFA DGFRYGYGTE VGISTNKIHA RGPMGLDGLT IYKYQLRGNG
QVASSYGVGP GKRAFKHTPI NIDNISQVSK K
