ID   PROA_AQUAE              Reviewed;         435 AA.
AC   O67166;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 141.
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=aq_1071;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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=AAC07119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000657; AAC07119.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70392; C70392.
DR   RefSeq; NP_213729.1; NC_000918.1.
DR   AlphaFoldDB; O67166; -.
DR   SMR; O67166; -.
DR   STRING; 224324.aq_1071; -.
DR   PRIDE; O67166; -.
DR   EnsemblBacteria; AAC07119; AAC07119; aq_1071.
DR   KEGG; aae:aq_1071; -.
DR   PATRIC; fig|224324.8.peg.833; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_0; -.
DR   InParanoid; O67166; -.
DR   OMA; PGVCNAM; -.
DR   OrthoDB; 223669at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
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..435
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189684"
SQ   SEQUENCE   435 AA;  49119 MW;  BE6500C58A2B2D61 CRC64;
     MNYIEEKVNR ARSVLRELTS LKTSVKNETL LKVAELIDKN RDYIKEENRK DVEKAKEMGL
     RPAVVDRLVL NDKRIDGMVK VLKDVASLPD PVGEIIKMWN LPNGLKVGRM RVPLGVIFIV
     YESRPNVTIE ASSLCMKSSN AVILRGGKEA INSNKALVNL IKEACRETGF PEDAVQFIDR
     SEREIVWEIL KMEGKIDVAI PRGGESLIRA VVEHAKVPVI KHYKGVCNIY VDDEADLEKA
     YHIVYNAKVQ RPSVCNAVEN LVINRKILKE FFPKMAYYLG KAGVELRCDE ESLQVIKENP
     KLSFVNAKPA TEEDYYEEFL DLILAVKVVD DVDEAIAFIE KYGSKHSDAI ITENYTKAMK
     FLREVDSAAV YVNASTRFTD GNEFGLGAEM GISTDKIHAR GPMALEELTI PKFVILGEGQ
     VRDNFGVPEE WMKEF