ID   PROA_ANAVT              Reviewed;         434 AA.
AC   Q3MH53;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   16-JUN-2009, entry version 26.
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;
DE            Short=GSA dehydrogenase;
GN   Name=proA; OrderedLocusNames=Ava_0057;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH dependent reduction of L-gamma-
CC       glutamyl 5-phosphate into L-glutamate 5-semialdehyde and
CC       phosphate. The product spontaneously undergoes cyclization to form
CC       1-pyrroline-5-carboxylate.
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 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family.
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DR   EMBL; CP000117; ABA19683.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_320578.1; -.
DR   GeneID; 3683469; -.
DR   GenomeReviews; CP000117_GR; Ava_0057.
DR   KEGG; ava:Ava_0057; -.
DR   NMPDR; fig|240292.3.peg.363; -.
DR   HOGENOM; Q3MH53; -.
DR   BioCyc; AVAR240292:AVA_0057-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00412; -; 1.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
FT   CHAIN         1    434       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000229992.
SQ   SEQUENCE   434 AA;  46945 MW;  3393756F7C3684DA CRC64;
     MTTLQVASSL NDIAQQTRQA ASLLAMLSTE AKNQAIAAVA QALESAKEEI LQANIADCEA
     ATAEGIAKPL YKRLQLDEHK LRDAIAGVRD VGKLADPIGQ VQIQRELDTG LVLKRITCPL
     GVLGIIFEAR PEAAIQIISL AIKSGNGVIL KCGKEAVRSC EAIVKAVKQG LSTTDVNPDV
     VQLLTTREET LELLRLDKYV DLIIPRGSNS FVRFVQENTR IPVLGHADGI CHVYIDKSAD
     IEKAIAVSVD AKVQYPAACN AIETLLVHHS IAAEFLPKVA QALAERQVEL KGDERTLQIL
     PEIAAATAID WETEYSDFIL SIKIVDSLTE AIAHINQYGS RHTDAIITED VAAVETFFGL
     VNSAGVFHNC STRFADGFRY GFGAEVGIST QQMPPRGPVG LEGLVTYKYQ MTGTGHIVAT
     YTGENAKPFT HQDF
//