P5CS_SOLLC
ID P5CS_SOLLC Reviewed; 717 AA.
AC Q96480;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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;
GN Name=PRO2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ailsa Craig;
RA Maggio A., Garcia-Rios M., Fujita T., Bressan R.A., Joly R.J.,
RA Hasegawa M.P., Csonka L.N.;
RT "Cloning of tomPRO1 and tomPRO2 from Lycopersicon esculentum L.:
RT coexistence of policistronic and monocistronic genes which encode the
RT enzymes catalyzing the first two steps of proline biosynthesis.";
RL (er) Plant Gene Register PGR96-077(1996).
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; U60267; AAB67875.1; -; mRNA.
DR PIR; T07422; T07422.
DR RefSeq; NP_001233907.1; NM_001246978.2.
DR AlphaFoldDB; Q96480; -.
DR SMR; Q96480; -.
DR STRING; 4081.Solyc08g043170.2.1; -.
DR PaxDb; Q96480; -.
DR GeneID; 544281; -.
DR KEGG; sly:544281; -.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR InParanoid; Q96480; -.
DR OrthoDB; 832430at2759; -.
DR UniPathway; UPA00098; UER00359.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q96480; baseline.
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; 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; cd04256; AAK_P5CS_ProBA; 1.
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; 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 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;
KW Reference proteome; Transferase.
FT CHAIN 1..717
FT /note="Delta-1-pyrroline-5-carboxylate synthase"
FT /id="PRO_0000109775"
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; 77590 MW; 1E206428B69EEBCA CRC64;
METVDSTRAF VKNVKRLIVK VGTAVVTRAD GRLALGRLGA LCEQLQELNS QGYEVILVTS
GAVGVGRQRL RYRKLLNSSF LDLQKPQTEL DGKACAAVGQ NGLMALYDSL FSQLDVTSAQ
LLVTDNDFRD PDFRRQLNDT VNSLLSLKVI PIFNENDAIS TRRAPYEDSS GIFWDNDSLA
ALLALELKAD LLVLLSDVDG LYSGPPRDPD SKLIYTYIKE IHERVITFGD KSRVGRGGMT
AKVKAAMYAA YAGIPVVITS GFATDNIIKV LHGERIGTLF HCDANKWASI GETDAREMAV
AARACSRRLQ ALSSQERSKI LQDIADALEA NEKAILAENE ADVVAAQQAG YEKSLISRLA
LNPGKISSLA NSVRVLSNMD EPLGHTLKRT EIADGFILEK SSSPLGVVLI IFESRPDALV
QIASLAVRSG NGLMLKGGKE AKRSNAILHK VITSAIPVSV GERLIGLVTS REEIPELLKL
DDVIDLVIPR GSNKLVSQIK ASTKIPVLGH ADGICHVYVD KSADMDMAKR ITVDAKIDYP
AACNAMETLL VHKDLAQNGG LNDLIVELQT KGVSLYGGPK ASSLLMIPEA RTFRHEYSSL
ACTVEVVEDV YAAIDHIHQH GSAHTDSIIT EDQEVAEVFL RQVDSAAVFH NASTRFSDGF
RFGLGAEVGI STGRIHARGP VGVEGLLTTK WLARGSGQIV DGDKSIVYSH KDLTQQG
