ID W1PJ72_AMBTC Unreviewed; 698 AA.
AC W1PJ72;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
GN ORFNames=AMTR_s00012p00263260 {ECO:0000313|EMBL:ERN08053.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN08053.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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}.
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; KI393609; ERN08053.1; -; Genomic_DNA.
DR AlphaFoldDB; W1PJ72; -.
DR STRING; 13333.W1PJ72; -.
DR EnsemblPlants; ERN08053; ERN08053; AMTR_s00012p00263260.
DR Gramene; ERN08053; ERN08053; AMTR_s00012p00263260.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_016144_0_0_1; -.
DR OMA; MGHAEGI; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR020593; G-glutamylP_reductase_CS.
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 NCBIfam; TIGR01027; proB; 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 PIRSF; PIRSF036429; P5C_syn; 1.
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 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:UP000017836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429}.
FT DOMAIN 2..241
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
SQ SEQUENCE 698 AA; 75310 MW; 93A2B3E879F3DD73 CRC64;
MVGTAVVTRS DGRLALGRVG ALCEQVKELN SQGLEVILVT SGAVGVGRQR LRYRRLVNSS
FADLQKPQLE LDGKACAAVG QNGLMALYDV LFSQLDVTSS QLLVTDNDFK DSDFRMQLTE
TVNSLLNLRV VPVFNENDAV STRRAPYEDS SGIFWDNDSL AALLALELKA DLLVLLSDVE
GLYSGPPGEP KSKLIHTYIK EKHYEKITFG DKSRVGRGGM TAKVKAAVYA ASAGTPVVIT
SGYSLDGVIK VLQGERVGTL FHQDAHLWAS SKEISAREMA IAARDCSRRL QTLSSEERRK
ILLGIADALE ANEALIKVEN DADVIAAQQA GYEKSLVSRL TLRPGKIASL AKNIRKLADM
EEPIGQVLKR TELADGLILE KTSSSLGVLL IVFESRPDAL VQIASLAVRS GNGLLLKGGK
EATRSNAVLH KVITAAIPES VGSKLIGLVT SRDEIPDLLK LDDVIDLVIP RGSNKLVSQI
KESTKIPVLG HADGICHVYV DKSANMDVAK SIVLDAKIDY PAACNAMETL LVHKHLTQTG
GLNELIQELK VEGVTIYGGP RASALLDLPQ ISSFHHEYNS LACTVEIVDD VFAAIDHIHR
HGSAHTECII AEDCEIAETF LHQVDSAAVF HNASTRFCDG ARFGLGAEVG ISTGRIHARG
PVGVEGLLTT RWILRGSGQV VDGDKRVVYT HKELPLHA
//
