ID   PROA_ANAD2              Reviewed;         427 AA.
AC   B8J8Z7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=A2cp1_0236;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001359; ACL63595.1; -; Genomic_DNA.
DR   RefSeq; WP_012631658.1; NC_011891.1.
DR   AlphaFoldDB; B8J8Z7; -.
DR   SMR; B8J8Z7; -.
DR   EnsemblBacteria; ACL63595; ACL63595; A2cp1_0236.
DR   KEGG; acp:A2cp1_0236; -.
DR   HOGENOM; CLU_030231_0_0_7; -.
DR   OMA; PGVCNAM; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000007089; 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..427
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_1000193564"
SQ   SEQUENCE   427 AA;  45198 MW;  6B63D12787C64B24 CRC64;
     MRKEKSLGLA AEMRKLAEAS REAARALSHA DPRRKDAALR AAAEAIGRRE KRILSENARD
     VAAARAAGQN AAYLDRLRLD PKRLAGIGAA LHEIAGLRDP VGEVTASWRR PNGLEIRKVR
     IPLGVVLMVY EARPNVTVDA AALCLKSGNA AILRPGSDAL RSSLALAAAF AEGLEKAGLP
     AASAQVVPTP DREATYELLA LDDLIDLAIP RGGPSLIRAV AARSRVPVLK HYQGVCHLYL
     DASAPPQQAV DLALNGKVQR PGVCNATECL LVHRGAAGKL LPPVGRALAD AGVELRCDPT
     ALTILKRAGV AAVPARPDDF GKEFLDKILA VRVVADLDGA LDHIARYGSL HTEAIVTRDL
     ASARRFQREV DASAVMVNAS TRFNDGGELG LGAEIGISTT KLHAFGPMGL AELTTQKFLV
     EGEGHVR