ID   P5CS_CAEEL              Reviewed;         800 AA.
AC   P54889;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 59.
DE   RecName: Full=Probable 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   ORFNames=T22H6.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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   -!- 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   -!- 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; Z50797; CAA90672.1; -; Genomic_DNA.
DR   PIR; T25140; T25140.
DR   RefSeq; NP_510133.1; -.
DR   UniGene; Cel.17267; -.
DR   HSSP; Q9WYC9; 1O20.
DR   Ensembl; T22H6.2; Caenorhabditis elegans.
DR   GeneID; 181417; -.
DR   WormBase; WBGene00011938; T22H6.2.
DR   WormPep; T22H6.2; CE03697.
DR   NextBio; 913848; -.
DR   ArrayExpress; P54889; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016163; Ald_DHase_C.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR001057; Glu_5kinase.
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; Complete proteome; Kinase;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Proline biosynthesis;
KW   Transferase.
FT   CHAIN         1    800       Probable delta-1-pyrroline-5-carboxylate
FT                                synthetase.
FT                                /FTId=PRO_0000109771.
FT   REGION        1    352       Glutamate 5-kinase.
FT   REGION      353    800       Gamma-glutamyl phosphate reductase.
SQ   SEQUENCE   800 AA;  86527 MW;  39223F4973368F00 CRC64;
     MFRATRCLRL PLRNSHINIL RPTQTELIKT RSSALAPYEK VSPITAVGAT PVGVGNGNYC
     TKTRQKHPLI NTRNDLKKAQ RVVVKLGSAV ITREDECGLA LGRLASIVEQ VSELQQSGRQ
     MLIVSSGAVA FGRQKLRQEL VMSMSMRQTL RGPSGMTADK RACAASGMPG LMSLYEQLFQ
     QYGITVAQVL LTKPDIDDDQ RRKNLQATIE SLLSLNIIPI VNANDAVAPD PKLNMHISDN
     DSLAARLSAE IEAELLIILS NVNGVYTGPP DLEGSRLLYT YVPSENSGVT FGANSKFGTG
     GMESKVTACV NALNNGVTTV ITNGLAQDAI TDAVAGKKIG TMFCNTKGYE GPPIEEVAEK
     CRDAGRQLAA LSNKERGAMV RHLAALLVDK EKYIIEANQT DLANAKSAGL DPQLLNRLKM
     TPEKIQDLHA GLNTIADSAE TLVGRVLKKV KISEGLFLEQ VTVPIGSLMV IFESRPDCLP
     QVASLAMASG NALLLKGGKE AEESNKALHA LVQEALGTHG FEMRDAVTLV RSREDVADLL
     QLKDLIDLII PRGSSDLVRS MQEKSKGIPV LGHAEGVWHV YIDKDCDEQK AIQIVRDSKC
     DYPSACNAAE TILIHKDLAT APFFDSLCSM FKAEGVKLHA GPKLAALLKF APPPAESMSF
     EYGSLECTLE VVDNVEEAVA HIIRYGSGHT ESIITENTNT AEHFLKHVDS ACAFHNASTR
     FADGYRFGLG AEVGISTGRI HARGPVGVEG LLTTKWLLRG EGHLVEDFKN GKYSYLHENL
     NPSEVYRALD AAGELKKATA
//