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Database: UniProt
Entry: A0A0E0PNE9_ORYRU
LinkDB: A0A0E0PNE9_ORYRU
Original site: A0A0E0PNE9_ORYRU 
ID   A0A0E0PNE9_ORYRU        Unreviewed;       755 AA.
AC   A0A0E0PNE9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthase {ECO:0000256|PIRNR:PIRNR036429};
DE   Includes:
DE     RecName: Full=Glutamate 5-kinase {ECO:0000256|PIRNR:PIRNR036429};
DE              Short=GK {ECO:0000256|PIRNR:PIRNR036429};
DE              EC=2.7.2.11 {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Gamma-glutamyl kinase {ECO:0000256|PIRNR:PIRNR036429};
DE   Includes:
DE     RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|PIRNR:PIRNR036429};
DE              Short=GPR {ECO:0000256|PIRNR:PIRNR036429};
DE              EC=1.2.1.41 {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036429};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI05G20150.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI05G20150.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC       osmoregulation in plants. {ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC         Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001844,
CC         ECO:0000256|PIRNR:PIRNR036429};
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,
CC         ECO:0000256|PIRNR:PIRNR036429};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005185, ECO:0000256|PIRNR:PIRNR036429}.
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|PIRNR:PIRNR036429}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC       phosphate reductase family. {ECO:0000256|ARBA:ARBA00006300,
CC       ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC       kinase family. {ECO:0000256|ARBA:ARBA00009302,
CC       ECO:0000256|PIRNR:PIRNR036429}.
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DR   AlphaFoldDB; A0A0E0PNE9; -.
DR   STRING; 4529.A0A0E0PNE9; -.
DR   EnsemblPlants; ORUFI05G20150.1; ORUFI05G20150.1; ORUFI05G20150.
DR   Gramene; ORUFI05G20150.1; ORUFI05G20150.1; ORUFI05G20150.
DR   eggNOG; KOG1154; Eukaryota.
DR   eggNOG; KOG4165; Eukaryota.
DR   HOGENOM; CLU_016144_0_0_1; -.
DR   OMA; HKYGSGH; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04256; AAK_P5CS_ProBA; 1.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   HAMAP; MF_00412; ProA; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
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; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR041744; G5K_ProBA.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR000965; GPR_dom.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   NCBIfam; TIGR01092; P5CS; 1.
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; PF00696; AA_kinase; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 2.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036429};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR036429};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036429};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..299
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   DOMAIN          333..595
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   755 AA;  81872 MW;  2328DB89D193BD78 CRC64;
     MASVDPSRSF VRDVKRVIIK IIRSGALLGL FCGLLDVTAY VEVANLSTLV GTAVVSRQDG
     RLALGRVGAL CEQVPNQRKV AMQVKELNSL GYEVILVTSG AVGVGRQRLR YRKLVNSSFA
     DLQKPQMELD GKACAAVGQS GLMALYDMLF NQLDVSSSQL LVTDSDFENP KFREQLTETV
     ESLLDLKVIP IFNENDAIST RKAPYEDSSG IFWDNDSLAG LLALELKADL LILLSDVDGL
     YSGPPSEPSS KIIHTYIKEK HQQEITFGDK SRVGRGGMTA KVKAAVLASN SGTPVVITSG
     FENRSILKVL HGEKIGTLFH KNANLWESSK DVSAREMAVA ARDCSRHLQN LSSEERKKIL
     LDVADALEAN EDLIRSENEA DVAAAQVAGY EKPLVARLTI KPGKIASLAK SIRTLANMED
     PINQILKKTE VADDLVLEKT SCPLGVLLIV FESRPDALVQ IASLAIRSGN GLLLKGGKEA
     IRSNTILHKV ITDAIPRNVG EKLIGLVTTR DEIADLLKLD DVIDLVIPRG SNKLVSQIKA
     STKIPVLGHA DGICHVYIDK SADMDMAKHI VMDAKIDYPA ACNAMETLLV HKDLMKSPGL
     DDILVALKTE GVNIYGGPIA HKALGFPKAV SFHHEYSSMA CTVEFVDDVQ SAIDHIHRYG
     SAHTDCIVTT DDKVAETFLR RVDSAAVFHN ASTRFSDGAR FGLGAEVGIS TGRIHARGPV
     GVEGLLTTRW ILRGRGQVVN GDKDVVYTHK SLPLQ
//
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