P5CS_ACTDE
ID P5CS_ACTDE Reviewed; 717 AA.
AC O04015;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate synthase;
DE Short=P5CS;
DE Includes:
DE RecName: Full=Glutamate 5-kinase;
DE Short=GK;
DE EC=2.7.2.11;
DE AltName: Full=Gamma-glutamyl kinase;
DE Includes:
DE RecName: Full=Gamma-glutamyl phosphate reductase;
DE Short=GPR;
DE EC=1.2.1.41;
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
OS Actinidia deliciosa (Kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=3627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Axillary bud;
RA Walton E.F., Podivinsky E., Wu R.-M., Reynolds P.H.S., Young L.W.;
RT "Regulation of proline accumulation in kiwifruit buds with and without
RT hydrogen cyanamide treatment.";
RL Physiol. Plantarum 102:171-178(1998).
CC -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC osmoregulation in plants.
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 -!- 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 -!- ACTIVITY REGULATION: Feedback regulated by proline.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in leaves and is inducible
CC in roots subjected to salt stress.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC phosphate reductase family. {ECO:0000305}.
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DR EMBL; U92286; AAC14481.1; -; mRNA.
DR AlphaFoldDB; O04015; -.
DR SMR; O04015; -.
DR UniPathway; UPA00098; UER00359.
DR UniPathway; UPA00098; UER00360.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036429; P5C_syn; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01092; P5CS; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS01223; PROA; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Proline biosynthesis; Transferase.
FT CHAIN 1..717
FT /note="Delta-1-pyrroline-5-carboxylate synthase"
FT /id="PRO_0000109774"
FT REGION 1..296
FT /note="Glutamate 5-kinase"
FT REGION 297..717
FT /note="Gamma-glutamyl phosphate reductase"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 236..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 717 AA; 77440 MW; BC76103DB08C6F8C CRC64;
MDAVDSTRAF VKGVKRVIIK VGTAVVTRAD GRLALGRLGA LCEQIHELNS QGFEVILVTS
GAVGVGRQRL RYRKLVNSSF ADLQKPQIEL DGKACAAVGQ NGLLALYDTL FSQLDVTSAQ
LLVTDNDFRD PEFRKQLTET VESLLNLKVI PIFNENDAVS TRKAPYEDAS GIFWDNDSLA
ALLALELKAD LLVLLSDVEG LYSGPPSDPQ SKLIHTYIKE MFEGLITFGD KSRVGRGGMT
AKVKAAVYAA HAGIPVVITS GYATNNIIKV LQGERIGTLF HRDAQKWAPV GDVGARDMAV
AARESSRRLQ AMSPQDRSKI LLDVADALEA NEKLIRIENE ADLAAAQQAG YEKSLISRLA
LKSGKISSLA KSIRVLANME EPIGHVLKRT EITDGLVLEK TSSPLGVLLI IFESRPDALV
QIASLAIRSG NGLVLKGGKE AKRSNAILHK VITSAIPENV GPRLIGLVTS REEIPDLLKL
DDVIDLVIPR GSNKLVSQIK ESTKIPVLGH ADGICHVYVD KSANMDMAKK VVLDAKTDYP
AACNAMETLL VHKDLVQNGC LDELIVELQI KGVVIHGGPR ASSLLHIPEA RSLHHEYSSL
ACTIEIVDDV YAAIDHIHRH GSAHTDSIIT EDHEVAEIFL RQVDSSSVLH NASTRFSDGA
RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIARGSGQVV DGDKGIVYTH KDLTSHA
