ID   PROA_RHORT              Reviewed;         427 AA.
AC   Q2RV06;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=Rru_A1238;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-
CC       phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC       spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
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DR   EMBL; CP000230; ABC22039.1; -; Genomic_DNA.
DR   RefSeq; WP_011388993.1; NC_007643.1.
DR   RefSeq; YP_426326.1; NC_007643.1.
DR   AlphaFoldDB; Q2RV06; -.
DR   SMR; Q2RV06; -.
DR   STRING; 269796.Rru_A1238; -.
DR   EnsemblBacteria; ABC22039; ABC22039; Rru_A1238.
DR   KEGG; rru:Rru_A1238; -.
DR   PATRIC; fig|269796.9.peg.1303; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_5; -.
DR   OMA; PGVCNAM; -.
DR   OrthoDB; 223669at2; -.
DR   PhylomeDB; Q2RV06; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..427
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000230021"
SQ   SEQUENCE   427 AA;  44758 MW;  42D85EDEA3A852EA CRC64;
     MNDAARLTTD DIPGLMIDIG RRARAAGRIL ALAPAAARNA ALLAGAAALR AEAGAIALEN
     AKDMSAGRAK GLTDALLDRL ELTPARIEAM AKGLEDIAAL PDPVGTVLAG WQRPNGLRIE
     RVRVPIGVIG VIYESRPNVT ADAGALCLKA GNAAILRGGS ESFNSSRAIH RCLAAGLRAA
     GLPEDAIQSV PTPDRAAVGM LLTMTDFIDV IVPRGGKSLI ERVSAESKVP LFKHLEGLCH
     TYIHAKADPQ KALSVTVNAK MRRTGVCGST ETILVDRAIA ATILPPLLDA LAKAGCALRG
     DEETRAFSER VGPATAEDWD TEYLDAIVSI RVVADLDEAL AHIAAHSSDH TDCILTEDAA
     AAERFLTEVD SAIVMHNAST QFADGGEFGM GAEIGISTGR LHARGPVGVE QLTIFKYKVR
     GTGQTRP