GenomeNet

Database: UniProt
Entry: A0A222FPL2_9GAMM
LinkDB: A0A222FPL2_9GAMM
Original site: A0A222FPL2_9GAMM 
ID   A0A222FPL2_9GAMM        Unreviewed;       418 AA.
AC   A0A222FPL2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CHH28_19550 {ECO:0000313|EMBL:ASP40730.1};
OS   Bacterioplanes sanyensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Bacterioplanes.
OX   NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP40730.1, ECO:0000313|Proteomes:UP000202440};
RN   [1] {ECO:0000313|EMBL:ASP40730.1, ECO:0000313|Proteomes:UP000202440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NV9 {ECO:0000313|EMBL:ASP40730.1,
RC   ECO:0000313|Proteomes:UP000202440};
RA   Rehman Z.U.;
RT   "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT   Sea.";
RL   Submitted (JUL-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP022530; ASP40730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222FPL2; -.
DR   KEGG; bsan:CHH28_19550; -.
DR   OrthoDB; 9809970at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000202440; Chromosome.
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:UP000202440}.
FT   DOMAIN          12..288
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          310..374
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   418 AA;  45077 MW;  8761FC92B9DC0380 CRC64;
     MNVTEYMHTL GQQARQASRA MARASSQDKN AALLAIAAEI ESRRETLKQA NANDMQRGRD
     NGLEAALLDR LELTDARIDT MVEGLHQVAS LTDPVGEITD LSYRPSGIQV GKMRVPLGVI
     GIIYESRPNV TIEAASLCLK SGNAAILRGG SEAIDSNRAL AECIRAGLQT AGLPAQAVQV
     VDTTDRAAVG ALITMPDYVD VIVPRGGKGL IERISREAQV TVIKHLDGIC HVYIDEFADL
     GKATNIAINA KTHRYGTCNT METLLVHQAV AEQILPDLAA AYRALDVELR GCERTCTLLS
     HALAATEQDW DTEYLAPILS IAIVDDLDAA IDHINRHGSH HTDSIVTENY TLARRFLTEV
     DSSSVMVNAS TRFADGFEYG LGAEIGISTD KIHARGPVGL EGLTSQKYVV LGNGEIRK
//
DBGET integrated database retrieval system