ID A0A0D3BQG1_BRAOL Unreviewed; 717 AA.
AC A0A0D3BQG1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=106342005 {ECO:0000313|EnsemblPlants:Bo4g025890.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo4g025890.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo4g025890.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo4g025890.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC osmoregulation in plants. {ECO:0000256|ARBA:ARBA00003492,
CC 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 RefSeq; XP_013636226.1; XM_013780772.1.
DR AlphaFoldDB; A0A0D3BQG1; -.
DR STRING; 109376.A0A0D3BQG1; -.
DR EnsemblPlants; Bo4g025890.1; Bo4g025890.1; Bo4g025890.
DR GeneID; 106342005; -.
DR Gramene; Bo4g025890.1; Bo4g025890.1; Bo4g025890.
DR KEGG; boe:106342005; -.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_016144_0_0_1; -.
DR OMA; MGHAEGI; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000032141; Chromosome C4.
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; 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; 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; 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:SF20; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE A; 1.
DR PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00171; Aldedh; 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:UP000032141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429}.
FT DOMAIN 15..260
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 291..558
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 717 AA; 77800 MW; E551447A7C7FC677 CRC64;
MEELDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS DGFEVILVSS
GAVGLGRQRL RYRQLVNSSF ADLQKPQHEL DGKACAGVGQ SSLMAYYETM FDQLDVTAAQ
LLVNDSSFRD KEFRKQLNET VKSMLDLRVI PIFNENDAIS TRRAPYQDSS GIFWDNDSLA
ALLALELKAD LLILLSDVEG LYTGPPSDPN SKLIHTFIKE KHQDEITFGD KSRLGRGGMT
AKVKAAVNAA YAGIPVIITS GYAAENIDKV LRGLRVGTLF HQDARLWAPI TDSTARDMAV
AARENSRKLQ ALSSEDRKQI LYAIADALEA NEKTIRAENE LDVATAQEAG LEESLVARLV
MTPAKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK TSSPLGVLLI VFESRPDALV
QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL
DDVIDLVIPR GSNKLVSQIK NTTKIPVLGH ADGICHVYVD KACNVDMAKR IVSDAKLDYP
AACNAMETLL VHKDLEQNAV LNELIFALQS NGVTLYGGPK ASKILNLPEA RSFNHEYCSK
SCTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDPEVAELFL RQVDSAAVFH NASTRFSDGF
RFGLGAEVGI STGRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGITYTH QDIPIQA
//
