ID PROA_ANADE Reviewed; 427 AA.
AC Q2IMG0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
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=Adeh_0212;
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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; CP000251; ABC79989.1; -; Genomic_DNA.
DR RefSeq; WP_011419272.1; NC_007760.1.
DR AlphaFoldDB; Q2IMG0; -.
DR SMR; Q2IMG0; -.
DR STRING; 290397.Adeh_0212; -.
DR KEGG; ade:Adeh_0212; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_7; -.
DR OrthoDB; 9809970at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000001935; 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 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; 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..427
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000252563"
SQ SEQUENCE 427 AA; 45377 MW; EA1F4626CCDB8EEB CRC64;
MRKEKSLGLA AEMRKLAEAS REAARALSHA DPRRKDAALR AAAEAIGRRE RRILSENARD
VAAARAAGQN AAYLDRLKLD PKRLAGIAAS LREIAGLRDP VGEVTASWRR PNGLEIRKVR
IPLGVVLMVY EARPNVTVDA AALCLKSGNA AILRPGSDAL RSSLALAEAF AEGLEKAGLP
AASAQVVPTP DREATYELLA LDDLIDLAIP RGGPSLIRAV AERSRVPVLK HYQGVCHLYL
DASAPPQQAV DLALNGKVQR PGVCNATECL LVHRAAAGKL LPPVGRALAD AGVELRCDPT
ALTILKRAGV AAVPARPDDF GKEFLDKILA VRVVADLDGA LDHIARYGSL HTEAIVTRDL
ASARRFQREV DASAVMVNAS TRFNDGGELG LGAEIGISTT KLHAFGPMGL AELTTQKFLV
EGEGHVR
//
