PROA_YEAST
ID PROA_YEAST Reviewed; 456 AA.
AC P54885; D6W321;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=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=PRO2; OrderedLocusNames=YOR323C; ORFNames=O6155;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lee J.M., Greenleaf A.L.;
RT "Mutations in Saccharomyces cerevisiae CTD kinase gene CTK1 are synthetic
RT lethals with mutant versions of SSD1 and PRO2.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- 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 -!- MISCELLANEOUS: Present with 6920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43565; AAA86261.1; -; Genomic_DNA.
DR EMBL; X90565; CAA62179.1; -; Genomic_DNA.
DR EMBL; Z75231; CAA99643.1; -; Genomic_DNA.
DR EMBL; AY692984; AAT93003.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11087.1; -; Genomic_DNA.
DR PIR; S58334; S58334.
DR RefSeq; NP_014968.1; NM_001183743.1.
DR PDB; 1VLU; X-ray; 2.29 A; A/B=1-456.
DR PDBsum; 1VLU; -.
DR AlphaFoldDB; P54885; -.
DR SMR; P54885; -.
DR BioGRID; 34709; 41.
DR DIP; DIP-6586N; -.
DR IntAct; P54885; 11.
DR MINT; P54885; -.
DR STRING; 4932.YOR323C; -.
DR iPTMnet; P54885; -.
DR MaxQB; P54885; -.
DR PaxDb; P54885; -.
DR PRIDE; P54885; -.
DR EnsemblFungi; YOR323C_mRNA; YOR323C; YOR323C.
DR GeneID; 854501; -.
DR KEGG; sce:YOR323C; -.
DR SGD; S000005850; PRO2.
DR VEuPathDB; FungiDB:YOR323C; -.
DR eggNOG; KOG4165; Eukaryota.
DR GeneTree; ENSGT00500000044903; -.
DR HOGENOM; CLU_030231_0_1_1; -.
DR InParanoid; P54885; -.
DR OMA; PGVCNAM; -.
DR BioCyc; YEAST:YOR323C-MON; -.
DR Reactome; R-SCE-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00360.
DR ChiTaRS; PRO2; yeast.
DR EvolutionaryTrace; P54885; -.
DR PRO; PR:P54885; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P54885; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IDA:SGD.
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; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..456
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189824"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 152..173
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:1VLU"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 292..305
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1VLU"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1VLU"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:1VLU"
SQ SEQUENCE 456 AA; 49740 MW; 7EDEC40C9B3DB07D CRC64;
MSSSQQIAKN ARKAGNILKT ISNEGRSDIL YKIHDALKAN AHAIEEANKI DLAVAKETGL
ADSLLKRLDL FKGDKFEVML QGIKDVAELE DPVGKVKMAR ELDDGLTLYQ VTAPVGVLLV
IFESRPEVIA NITALSIKSG NAAILKGGKE SVNTFREMAK IVNDTIAQFQ SETGVPVGSV
QLIETRQDVS DLLDQDEYID LVVPRGSNAL VRKIKDTTKI PVLGHADGIC SIYLDEDADL
IKAKRISLDA KTNYPAGCNA METLLINPKF SKWWEVLENL TLEGGVTIHA TKDLKTAYFD
KLNELGKLTE AIQCKTVDAD EEQDFDKEFL SLDLAAKFVT STESAIQHIN THSSRHTDAI
VTENKANAEK FMKGVDSSGV YWNASTRFAD GFRYGFGAEV GISTSKIHAR GPVGLDGLVS
YQYQIRGDGQ VASDYLGAGG NKAFVHKDLD IKTVTL
