PROA2_SYNY3
ID PROA2_SYNY3 Reviewed; 420 AA.
AC Q55167;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Gamma-glutamyl phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GPR 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
GN Name=proA2 {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=sll0461;
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; BAA10306.1; -; Genomic_DNA.
DR PIR; S74388; S74388.
DR AlphaFoldDB; Q55167; -.
DR SMR; Q55167; -.
DR IntAct; Q55167; 1.
DR STRING; 1148.1001164; -.
DR PaxDb; Q55167; -.
DR EnsemblBacteria; BAA10306; BAA10306; BAA10306.
DR KEGG; syn:sll0461; -.
DR eggNOG; COG0014; Bacteria.
DR OMA; GNCYLYW; -.
DR PhylomeDB; Q55167; -.
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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..420
FT /note="Gamma-glutamyl phosphate reductase 2"
FT /id="PRO_0000189825"
SQ SEQUENCE 420 AA; 45772 MW; 7EF77A46AD5C6F5F CRC64;
MTSDDAAAGL VRVLDAAQGA FLALDSYGGN DRSRAVLAMA EALERSFAQI LEANTLDLVV
SREMSVADCL CEWLKLTPER LQNTVTILKR LASLPDPLQR VMASPYQFNL AQTYCQLMPL
GVVALVYESF PELAAIAAGF CLKTGNSLVL RSCGASSHST AAICEILREG LLDADLPVDS
VSHIPSETSP NVQDLVGNAS QLNLVIPYGR PSFVEQISQQ CTPPVLKAAM GNCYLYWSSK
GDLEMVRQMI IDSHVGHPDP VNAIEKVLVS PGQNPAPLVR LLNNLQAKGF KLRGDAELCE
QFPDHLTLAK ENEWGKAYLD RTVAFRTTQN LKTAIAWINS HSSGHGDCIA TDSYQESRQF
SMGVDSALVY VNIPPYFCRN PRHGESLFLG VSSQKGQRRG LIGLEAFMTP KQIVQGESRS
