ID A0A2K2FHB6_9FIRM Unreviewed; 414 AA.
AC A0A2K2FHB6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CDQ84_06485 {ECO:0000313|EMBL:PNU00328.1};
OS Pseudoclostridium thermosuccinogenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoclostridium.
OX NCBI_TaxID=84032 {ECO:0000313|EMBL:PNU00328.1, ECO:0000313|Proteomes:UP000236151};
RN [1] {ECO:0000313|EMBL:PNU00328.1, ECO:0000313|Proteomes:UP000236151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5806 {ECO:0000313|EMBL:PNU00328.1,
RC ECO:0000313|Proteomes:UP000236151};
RA Koendjbiharie J.G., van Kranenburg R.;
RT "Investigating the central metabolism of Clostridium thermosuccinogenes.";
RL Submitted (JUN-2017) 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:PNU00328.1}.
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DR EMBL; NIOJ01000012; PNU00328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2FHB6; -.
DR KEGG; cthd:CDO33_14100; -.
DR OrthoDB; 9809970at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000236151; 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:UP000236151}.
FT DOMAIN 10..284
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 315..377
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 414 AA; 44795 MW; 71F2D53F13B098A6 CRC64;
MDELILKGEK AKKASYKLAN LSSLIKDDAL KKMSELLIKE KAKILEANAI DVQNAVDRGI
KGALIDRLTL NEKRIAAMAE GLLQIAALPD PVGEVVSMWK RPNGLQIGQK RVPIGVVGMI
YEARPNVTVD AAGLCIKSGN AVILRGGSEA INSNKAIISV IDTALAEAGM PEGTVQLIED
TSRETVARMM KLNKYIDVLI PRGGEGLINS VVQNSTVPVI QTGTGNCHVY VDGDADLDMA
ERIIVNAKTS RPGVCNAAET MLVDEAVAQE FLPKVLKTLQ GLNVEIRGCE RTRAIYSDCL
PAAEEDWDKE YLDYILAVKV VGGIDEAIDH INRHGTKHSE AIVTTNYNKA QRFLNEIDAA
AVYVNASTRF TDGGEFGFGA EIGISNQKLH ARGPVGLKEL TTIKYIIYGE GQIR
//
