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Database: UniProt
Entry: A0A1R4AZZ4_9VIBR
LinkDB: A0A1R4AZZ4_9VIBR
Original site: A0A1R4AZZ4_9VIBR 
ID   A0A1R4AZZ4_9VIBR        Unreviewed;       418 AA.
AC   A0A1R4AZZ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, 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   ECO:0000313|EMBL:SJL82229.1};
GN   ORFNames=VPAL9027_00140 {ECO:0000313|EMBL:SJL82229.1};
OS   Vibrio palustris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1918946 {ECO:0000313|EMBL:SJL82229.1, ECO:0000313|Proteomes:UP000189475};
RN   [1] {ECO:0000313|EMBL:SJL82229.1, ECO:0000313|Proteomes:UP000189475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 9027 {ECO:0000313|EMBL:SJL82229.1,
RC   ECO:0000313|Proteomes:UP000189475};
RA   Peterson S.W.;
RL   Submitted (FEB-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}.
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DR   EMBL; FUFT01000001; SJL82229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4AZZ4; -.
DR   STRING; 1918946.VPAL9027_00140; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000189475; 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; 1.
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:UP000189475}.
FT   DOMAIN          7..281
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   418 AA;  44773 MW;  7BB5A1CC3AD71BDE CRC64;
     MNVDLTNMGK AAKDAAFQLA VTPTEQKNRA LALIADELEA NAATILAANQ QDISKGKEAG
     LSDAMLDRLL LTEDRLSAIA NDVRNVIMLN DPVGSEVDSK VLGNGMSLSR RRVPLGVIGV
     IYEARPNVTI DIAALCLKTG NASILRGGKE TFASNMELVK VIQNALQKAE LPAASVQYIE
     KPDRELVSQL LTLDEYVDMI IPRGGAGLHK MCKENSSIPV IIGGFGISHM YIDDTADLAR
     SVAVVDNAKT QRPSACNSLD TLLIHESVAE QFCAQLIDAM GERVTFVADD SAVSLLQSAP
     RVRSAQDGDF DTEWLDYVLG VKVVTGVQAA IEHMRIHNAS HSDAIMTNSL DNAEAFINSA
     GSAAVYVNAS TRFTDGAQFG LGAEVAVSTQ KLHARGPMGL EELTSYKWVG KANYLVRS
//
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