ID   PROA_HYDS0              Reviewed;         441 AA.
AC   B4U8A0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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};
GN   OrderedLocusNames=HY04AAS1_0674;
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC   unclassified Hydrogenobaculum.
OX   NCBI_TaxID=380749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y04AAS1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001130; ACG57361.1; -; Genomic_DNA.
DR   RefSeq; WP_012513717.1; NC_011126.1.
DR   AlphaFoldDB; B4U8A0; -.
DR   SMR; B4U8A0; -.
DR   STRING; 380749.HY04AAS1_0674; -.
DR   EnsemblBacteria; ACG57361; ACG57361; HY04AAS1_0674.
DR   KEGG; hya:HY04AAS1_0674; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_0; -.
DR   OMA; PGVCNAM; -.
DR   OrthoDB; 223669at2; -.
DR   UniPathway; UPA00098; UER00360.
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.
FT   CHAIN           1..441
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_1000193616"
SQ   SEQUENCE   441 AA;  49698 MW;  CC7369139E0B431C CRC64;
     MKEYALEIAT KAKAVLPKLS SLNPAVKNSI LIRVSQLLKE NKELIQKENE KDIEFAKSIN
     LSKAMIDRLK VGEKQINGMI KILEDVAKLK DPVGEITSMW TVDNGLKIGR MRVPLGVIFI
     IYESRPNVTI EAASLCFKSS NAVILRGGKE AIHTNKILSD LFRQAIREHV EGLEDAVCFV
     DKREREIVTE LLQLEGLVDV AIPRGGESLI KAVSETAKIS VIKHYKGVCS IYVDNEADLK
     KAYNIVYNAK VQRPSVCNAI ENLVIHKDLL QDFWPKMAMV LLESDVELRC DEDSYEILQN
     KDFDSFKSKI KKATEKDYYE EFLDLILAVK TVNSLEEAMQ FIEKYGSKHS DAIITENHTK
     AMRFLQEVDS AAVYVNASTR FTDGNEFGLG AEMGISTDKI HARGPMALRE LTIEKFIIFG
     NGQLRENVGI PKELKEKLQI D