PROA1_SYNY3
ID PROA1_SYNY3 Reviewed; 433 AA.
AC P54902;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Gamma-glutamyl phosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GPR 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00412};
GN Name=proA1 {ECO:0000255|HAMAP-Rule:MF_00412}; Synonyms=proA;
GN OrderedLocusNames=sll0373;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10399.1; -; Genomic_DNA.
DR PIR; S76553; S76553.
DR AlphaFoldDB; P54902; -.
DR SMR; P54902; -.
DR STRING; 1148.1001665; -.
DR PaxDb; P54902; -.
DR EnsemblBacteria; BAA10399; BAA10399; BAA10399.
DR KEGG; syn:sll0373; -.
DR eggNOG; COG0014; Bacteria.
DR InParanoid; P54902; -.
DR OMA; PGVCNAM; -.
DR PhylomeDB; P54902; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..433
FT /note="Gamma-glutamyl phosphate reductase 1"
FT /id="PRO_0000189801"
SQ SEQUENCE 433 AA; 46350 MW; 41C590A10DC90283 CRC64;
MVISPSLSAL HTLAHNARQA ALHLGSLNTA ERNQAIAAIA DGLTAAMPEI LAANQEDCAA
AEAMGIAKPL YNRLLLGESK LKSTIAGVKD VEHLPDPLGQ VTLHRQLDEG LVLKRVGCPL
GVLGVIFEAR PEALIQISSL AIKSGNAVIL KGGREATRSC QVLTEVIQTA LAKTVVSPEA
INLLTTREEI RELLGLNQYV DLIIPRGSNE FVQYIQQNTQ IPVLGHADGI CHLYLDAQAD
LSKAIPITVD AKTQYPAACN AIETLLVHQA IAAEFLPPLA QALGEKGVSL RGDSGTQKLI
DCEPATEADW CTEYSDLILS IKIVDSLEAA IDHINQYGSK HTDGIISEDL TAAEQFCQRV
DSAGVYHNCS TRFADGFRYG FGAEVGISTQ KMPPRGPVGL EGLVTYKYQL WGHGHIAATY
TGQGAKAFTH LDL
