ID   G4QJ27_BRUN1            Unreviewed;       415 AA.
AC   G4QJ27;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   10-JUN-2026, entry version 66.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000256|HAMAP-Rule:MF_00412,
GN   ECO:0000313|EMBL:AEP28895.1};
GN   OrderedLocusNames=GNIT_0751 {ECO:0000313|EMBL:AEP28895.1};
OS   Brumicola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064)
OS   (Glaciecola nitratireducens).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Alteromonadaceae; Brumicola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP28895.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP28895.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(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:0000256|HAMAP-Rule:MF_00412}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl
CC         5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066,
CC         ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00049024, ECO:0000256|HAMAP-
CC         Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00412}.
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DR   EMBL; CP003060; AEP28895.1; -; Genomic_DNA.
DR   RefSeq; WP_014107770.1; NC_016041.1.
DR   AlphaFoldDB; G4QJ27; -.
DR   STRING; 1085623.GNIT_0751; -.
DR   KEGG; gni:GNIT_0751; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_6; -.
DR   OrthoDB; 9809970at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000009282; 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-UniRule.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   FunFam; 3.40.309.10:FF:000006; Gamma-glutamyl phosphate reductase; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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   NCBIfam; NF001221; PRK00197.1; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00412};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW   Rule:MF_00412}; Reference proteome {ECO:0000313|Proteomes:UP000009282}.
FT   DOMAIN          7..273
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   415 AA;  45220 MW;  76916448BB2540A5 CRC64;
     MSLIKDLSRK AAEAAQILSV LDEAEKNAVL MDMAKTLRDN ANGIIENNAK DLVNAKNNDL
     AASMIDRLTL NQERIEAMAE GLETVAILPD PVGVERDLGT RPNGLQIRKM RVPLGVVCMI
     YEARPNVTAD AAGLCFKSGN AAILRGGKEA LESSLFIANL LQDVLEKHNL PRELISVVPN
     ADRALMQELM EQKDYIDVII PRGGEGLINY VTENSKVPVI QHFKGVCHLY IDKEADIETA
     INLLVNGKTQ RTGVCNALEG LLVHEDIAEE FLSVAGPILE EHSVKVNSCE NSSKYFNNST
     VIKTDGFGEE YLDLEIAVRI VPTIEGAMQH IARFGSHHTE VICTKNELTA KRFQRTVDSS
     VVMVNASSRF SDGSQLGLGA EIGIATTKLH AYGPMGLESL TTEKYLVNGV GQVRA
//