ID A0A0P7E8X2_9GAMM Unreviewed; 427 AA.
AC A0A0P7E8X2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN Name=proA {ECO:0000256|HAMAP-Rule:MF_00412};
GN ORFNames=AOG28_01075 {ECO:0000313|EMBL:KPM82011.1};
OS Cobetia sp. UCD-24C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Cobetia.
OX NCBI_TaxID=1716176 {ECO:0000313|EMBL:KPM82011.1, ECO:0000313|Proteomes:UP000050261};
RN [1] {ECO:0000313|EMBL:KPM82011.1, ECO:0000313|Proteomes:UP000050261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-24C {ECO:0000313|EMBL:KPM82011.1,
RC ECO:0000313|Proteomes:UP000050261};
RA Krusor M., Coil D.A., Lang J.M., Eisen J.A., Alexiev A.;
RT "Draft Genome of Cobetia sp. UCD-24C.";
RL Submitted (SEP-2015) 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:0000256|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:0000256|ARBA:ARBA00000979, ECO:0000256|HAMAP-
CC Rule:MF_00412};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_00412}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM82011.1}.
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DR EMBL; LJTD01000001; KPM82011.1; -; Genomic_DNA.
DR RefSeq; WP_054555035.1; NZ_LJTD01000001.1.
DR AlphaFoldDB; A0A0P7E8X2; -.
DR STRING; 1716176.AOG28_01075; -.
DR PATRIC; fig|1716176.3.peg.228; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000050261; Unassembled WGS sequence.
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; 2.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00412};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_00412}; Reference proteome {ECO:0000313|Proteomes:UP000050261}.
FT DOMAIN 20..297
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 312..383
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 427 AA; 45812 MW; EA3C53D7C7EF3181 CRC64;
MSEQGKHDTT DVVAYMNRLG HAARAASVVM RRVDSGIKNR ALQTMARLID ERRETLAEAN
AEDLARARAN GLSEAMVDRL ALTPARIDGM IEGLEQVAAL PDPVGEVDGL RSRPSGIQVG
HMRVPLGVIG IIFESRPNVT IEAASLCLKS GNACILRGGS EAASSNRALS EIISEALVLS
ELPATAVQVV ATTDRAAVGE LIAMPEFVDV IIPRGGKSLI SRISRDARVP VIKHLDGICH
VYIDATADLA MAVRIAENAK THRYGTCNTM ETLLVDAPVA AEVLPRIAER LAAHEVEIRG
CERTCEVLPQ AVAASAEDWD TEYLAPILAI RVVDGVDEAM AHIERHSSGH TEAIITENYA
LARRFMAEVD SSSVMVNAST RFADGFEYGL GAEIGISTDK LHARGPVGLE GLTTRKYIVF
GDGQIRQ
//
