ID   PROA_TRIV2              Reviewed;         434 AA.
AC   Q3MH53;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 94.
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=Ava_0057;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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=ABA19683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000117; ABA19683.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q3MH53; -.
DR   SMR; Q3MH53; -.
DR   STRING; 240292.Ava_0057; -.
DR   EnsemblBacteria; ABA19683; ABA19683; Ava_0057.
DR   KEGG; ava:Ava_0057; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_1_3; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000002533; 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-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..434
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000229992"
SQ   SEQUENCE   434 AA;  46945 MW;  3393756F7C3684DA CRC64;
     MTTLQVASSL NDIAQQTRQA ASLLAMLSTE AKNQAIAAVA QALESAKEEI LQANIADCEA
     ATAEGIAKPL YKRLQLDEHK LRDAIAGVRD VGKLADPIGQ VQIQRELDTG LVLKRITCPL
     GVLGIIFEAR PEAAIQIISL AIKSGNGVIL KCGKEAVRSC EAIVKAVKQG LSTTDVNPDV
     VQLLTTREET LELLRLDKYV DLIIPRGSNS FVRFVQENTR IPVLGHADGI CHVYIDKSAD
     IEKAIAVSVD AKVQYPAACN AIETLLVHHS IAAEFLPKVA QALAERQVEL KGDERTLQIL
     PEIAAATAID WETEYSDFIL SIKIVDSLTE AIAHINQYGS RHTDAIITED VAAVETFFGL
     VNSAGVFHNC STRFADGFRY GFGAEVGIST QQMPPRGPVG LEGLVTYKYQ MTGTGHIVAT
     YTGENAKPFT HQDF