ID   P5CS_MESCR              Reviewed;         719 AA.
AC   O65361;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
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;
GN   Name=P5CS;
OS   Mesembryanthemum crystallinum (Common ice plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalowski C.B., Quigley-Landreau F., Bohnert H.J.;
RT   "Mesembryanthemum crystallinum pyrroline-5-carboxylate synthetase
RT   mRNA.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; AF067967; AAC18862.1; -; mRNA.
DR   PIR; T12258; T12258.
DR   HSSP; Q9WYC9; 1O20.
DR   BRENDA; 1.2.1.41; 2210.
DR   BRENDA; 2.7.2.11; 2210.
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    719       Delta-1-pyrroline-5-carboxylate
FT                                synthetase.
FT                                /FTId=PRO_0000109776.
FT   REGION        1    293       Glutamate 5-kinase.
FT   REGION      294    719       Gamma-glutamyl phosphate reductase.
SQ   SEQUENCE   719 AA;  77855 MW;  1510D11AF5559961 CRC64;
     MDATRAFVKD VKRVVVKVGT AVVTRSDGRL ALGRLGSLCE QLKELNSDGY EVILVTSGAV
     SAGRQRLRFR KLVNSSFADL QKPQVELDGK ACAAVGQNGL MALYDTLFSQ LDLTAAQLLV
     TDNDFRDPSF RTQLTETVYQ LLDLKVVPVL NENDAVSTRK APYEDSSGIF WDNDSLAALL
     ALELKADLLI LLSDVDGLYN GPPSDPRSKL ISTYVKEKHQ GEITFGDKSR LGRGGMTAKV
     KAAVYAAYAG IPVIIASGKA TDNIIKVIDG QCVGTLFHKD AHLWVQVKET GVRDMAVAAR
     ESSRRLQAVS SEERKKILLD IADALEANEE KILAENEADV AAAQYAGYDR SLVARLAMNP
     DKISSLAKSI RVLADMEEPI GRILKRTEIA DGLILEKTSC PLGVLLIVFE SRPDALVQIA
     SLAIRSGNGL LLKGGKEAKR SNAILHKVIT SAIPDKVGEK LIGLVTSRDE IPDLLKLDDV
     IDLVIPRGSN KLVSQIKEST RIPVLGHADG ICHVYVDKSA NMDMAKRIVL DAKTDYPAAC
     NAMETLLVHK DLAENGGLND LIVDLRTEGV TMFGGPRIDA LQEFNIQATQ TFNREYSSPA
     CTVEIVDDVY AAIEHINHHG SAHTDCIIAE DHKVAETFLQ LVDSAAVLHN ASTRFCDGFR
     FGLGAEVGIS TSRIHARGPV GVEGLLTTRW VLKGSGQVVH GDKGVVYTHK DLPLVAQNS
//