ID   PROA_BART1              Reviewed;         409 AA.
AC   A9IMB2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   28-JAN-2026, entry version 99.
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=BT_0174;
OS   Bartonella tribocorum (strain DSM 28219 / CCUG 45778 / CIP 105476 / IBS
OS   506).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28219 / CCUG 45778 / CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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 + 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: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=CAK00658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM260525; CAK00658.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012230522.1; NC_010161.1.
DR   AlphaFoldDB; A9IMB2; -.
DR   SMR; A9IMB2; -.
DR   KEGG; btr:BT_0174; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_5; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001592; 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   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; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..409
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000340872"
SQ   SEQUENCE   409 AA;  44016 MW;  799420BB60213866 CRC64;
     MGQKARSAAA ALAVASSEQK NNALEMIALS LEAHSDEILR ANCLDLEKAT QNNLKAAMVD
     RLKLDELRLA AMIDSVRQVA RLSDPVGQIM SAWTRPNGLH ISRVRTPLGV IGIIYESRPN
     VTIDASSLCL KAGNAVILRG GSDSFHSSYA LHCALVQGLE HSGLPKSAIQ MVGTTDRAAV
     GEILKGLDGA IDVIVPRGGK SLVARVQSDA RVPVFAHLEG LCHIYIDKSA DLDMARNIVL
     NAKLRRTGIC GAVETVLIDN EALKKFLPVL TALQEKGCEI RATEDIAFLV PDVKLASEED
     WSHEYLDAIL SVKTVEGVEG AISHIKRYSS GHTESIIAED MEVVKKFFNH LDSAILLHNA
     STQFADGGEF GFGMEIGIAT GKMHARGPIG VEQLTSFQYH IKGNGQVRA
//