PROA_MEIRU
ID PROA_MEIRU Reviewed; 417 AA.
AC O86053;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 100.
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};
OS Meiothermus ruber.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Meiothermus.
OX NCBI_TaxID=277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=40;
RA Yaklichkin S.Y., Zimina M.S., Yurchenko Y.V., Hromov I.S., Neumivakin L.V.;
RT "Molecular cloning and sequence analysis of the proA gene from thermophilic
RT eubacterium Thermus ruber.";
RL Submitted (AUG-1998) 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; AF082661; AAC72811.1; -; Genomic_DNA.
DR AlphaFoldDB; O86053; -.
DR SMR; O86053; -.
DR UniPathway; UPA00098; UER00360.
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..417
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189748"
SQ SEQUENCE 417 AA; 44986 MW; A280A8A7E9C92268 CRC64;
MVTSPELKAY AQAARAAARA LSTASPRAKN TALLAIAAKL EAQQEALFAA NREDLEAAQA
AGLSKAKLDR LRLDEKVLRD LRTGLQQVAE MPDPVGEIEG LQIRPNGLQV GRMRVPLGVI
GFIYESRPNA TVEASALCLK AGNAILLRGG KEAWHSNRAL VGLMQAALQE AGLPREAIQL
VPTTDRSAIL EMCHLADLLD LIIPRGGRGL IELVQREARI PVLAHTEGIN HLFVDESTDP
GCAVQIALNG KTQRPSTCNS LEKVLVHQRI APVFLPMLAQ AMQKAGVELR GDEATCALIP
ARPATPEDWQ TEYLDLILTV KVVNSLEEAL EHIARYGSHH TEAICTNHHA HAMRFLREVD
ASLVLVNASP RFNDGFQLGL GAEIGISTSK LHAYGPMGVK ELTTTKFVAL GSGQVRD
