ID   PROA_ALIF1              Reviewed;         418 AA.
AC   Q5E6W0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 110.
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=VF_0741;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW85236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000020; AAW85236.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_047863672.1; NC_006840.2.
DR   RefSeq; YP_204124.1; NC_006840.2.
DR   AlphaFoldDB; Q5E6W0; -.
DR   SMR; Q5E6W0; -.
DR   STRING; 312309.VF_0741; -.
DR   EnsemblBacteria; AAW85236; AAW85236; VF_0741.
DR   KEGG; vfi:VF_0741; -.
DR   PATRIC; fig|312309.11.peg.734; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_6; -.
DR   OrthoDB; 223669at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000000537; Chromosome I.
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..418
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189808"
SQ   SEQUENCE   418 AA;  44790 MW;  711EFF9619D78FC5 CRC64;
     MNLTTMGQAA KAAAFDLAVA PTAQKNKALA IIADELEANK DAILAANEKD IKAAVEAGIS
     EAMQDRLLLT EERLVGIAND VRNVINLNDP VGSEIDSKVL ENGMSLSRRR VPIGVIGVIY
     EARPNVTIDI ASLCLKTGNA SILRGGKETF FSNMELVKVI QVALEKAGLP AASVQYIEKP
     DRELVSQLLT MDDYVDMIIP RGGAGLHKMC KENSSIPVII GGFGISHAFV DESADLERAL
     VVVDNSKAQR PSACNALDTL LVHEAVAPQF LALLANNMAG RVELVAEPKA YGLLKEFEGV
     SLREAQEGDF DTEWLSYTLG VKVVADVNEA AAHMQKHNAS HSDTILTNNI ESAEKFINTA
     GSAAVYVNAS TRFTDGAQFG LGAEVAVSTQ KLHARGPMGL EELTSYKWVG KADYLIRS