ID K9SR85_9SYNE Unreviewed; 428 AA.
AC K9SR85;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=Syn7502_00309 {ECO:0000313|EMBL:AFY72476.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72476.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY72476.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72476.1,
RC ECO:0000313|Proteomes:UP000010385};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL Submitted (MAY-2012) 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; CP003594; AFY72476.1; -; Genomic_DNA.
DR RefSeq; WP_015167135.1; NC_019702.1.
DR AlphaFoldDB; K9SR85; -.
DR STRING; 1173263.Syn7502_00309; -.
DR KEGG; synp:Syn7502_00309; -.
DR PATRIC; fig|1173263.3.peg.312; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_1_3; -.
DR OrthoDB; 9809970at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000010385; 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; 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:UP000010385}.
FT DOMAIN 7..282
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 428 AA; 46012 MW; D91396919DAE6AE4 CRC64;
MRSLLETVQI TKSAARSLAK LDHAAKNSAL EAIADAVNNH ADQILEANAQ DVENAVAANL
AAPLISRLKL NPNKVKAMAV GVRDVARLSD PTGIRQIHRE LDTGLILERI TCPLGVLGVI
FEARPDAVTQ IAALAIKSGN GVLLKGGSEA VLSCEAIAKI IHKALQTSAV APEVVQLLTT
RSETMEILKM DRHIDLIIPR GSNDFVRFIQ ANTNIPVLGH ADGICHLYVD QTVDIDQAVA
IAVDSKTQYP SACNAIETLL IHRAIAPEFL AKVIPALQAQ NVELRGCDQT LSLYPDLIPA
TETDWATEYC DLILSIKIVD SLESAIDHIN TFGSKHTEAI ATTNPEVATI FASDVDAAGV
YHNCSTRFAD GFRYGFGAEV GISTQKMPPR GPVGLEGLVT YKYHLQGHGQ IVADYSGSNP
KSFIHRDI
//
