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   16-JUN-2009, entry version 61.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthetase;
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
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
CC       to osmoregulation in plants.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH.
CC   -!- ENZYME REGULATION: Feedback regulated by proline.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in leaves and is
CC       inducible in roots subjected to salt stress.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC       kinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gamma-
CC       glutamyl phosphate reductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U92286; AAC14481.1; -; mRNA.
DR   HSSP; Q9WYC9; 1O20.
DR   BRENDA; 1.2.1.41; 67098.
DR   BRENDA; 2.7.2.11; 67098.
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:EC.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR001057; Glu_5kinase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   InterPro; IPR005715; ProB.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
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;
KW   NADP; Nucleotide-binding; Oxidoreductase; Proline biosynthesis;
KW   Transferase.
FT   CHAIN         1    717       Delta-1-pyrroline-5-carboxylate
FT                                synthetase.
FT                                /FTId=PRO_0000109774.
FT   REGION        1    296       Glutamate 5-kinase.
FT   REGION      297    717       Gamma-glutamyl phosphate reductase.
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
//