P5CS_VIGAC
ID P5CS_VIGAC Reviewed; 671 AA.
AC P32296;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Vigna aconitifolia (Moth bean) (Phaseolus aconitifolius).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3918;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1384052; DOI=10.1073/pnas.89.19.9354;
RA Hu C.-A.A., Delauney A.J., Verma D.P.S.;
RT "A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase)
RT catalyzes the first two steps in proline biosynthesis in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9354-9358(1992).
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; M92276; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A46295; A46295.
DR AlphaFoldDB; P32296; -.
DR SMR; P32296; -.
DR SABIO-RK; P32296; -.
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; 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 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..671
FT /note="Delta-1-pyrroline-5-carboxylate synthase"
FT /id="PRO_0000109778"
FT REGION 1..297
FT /note="Glutamate 5-kinase"
FT REGION 298..671
FT /note="Gamma-glutamyl phosphate reductase"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 237..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 671 AA; 73291 MW; 30BAE7AAF7ED1DA6 CRC64;
MESAVDPSRG FMKDVKRVII KVGTAVVTRE EGRLAVGRLG ALCEQIKQLN SLGYDIILVS
SGPVGIGRQR LRFRKLINSS FADLQKPQLE LDGKACAAVG QNSLMALYDT LFTQLDVTSA
QLLVTDNDFR DKDFRKQLTE TVKSLLALKV IPVFNENDAV STRKAPYEDS SGIFWDNDSL
SALLALELKA DLLVLLSDVE GLYSGPPSDP HSKLIYTYNK EKHQNEITFG DKSRVGRGGM
TAKVKAAVHA AEAGIPVVIT SGFAPENIIN VLQGQRIGTL FHKDAHEWAQ VKEVDAREMA
VAAGNVREGS RRYLQRKGNK ILLKIADALE ANEKIIRIEN EADVTAAQEA GYEKSLVARL
ALKPGKIASL ANNMRIIANM EDPIGRVLKR TELSDGLILE KTSSPLGVLL IVFESRPDAL
VQIASLAIRS GNGLLLKGGK EAKRSNAILH KVIIEAIPDN VGGKLIGLVT SREEIPELLK
LDDVIDLVIP RGSNKLVSQI KSSTKIPVLG HADGICHVYV DKSANVEMAK RIVLDAKVDY
PAACNAMETL LIHKDLIEKG WLKEIILDLR TEGVILYGGP VASSLLNIPQ AHSFHHEYSS
LACTAEIVDD VYAAIDHINL YGSAHTDSIV AEDNEVANVF LRQVDSAAVF HNASTRFSDG
ARFETRRRGW N
