ID   PROA_BIFLO              Reviewed;         431 AA.
AC   Q8G5H9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   16-JUN-2009, entry version 44.
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=BL1034;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24839.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_696203.1; -.
DR   HSSP; Q9WYC9; 1O20.
DR   GeneID; 1022561; -.
DR   GenomeReviews; AE014295_GR; BL1034.
DR   KEGG; blo:BL1034; -.
DR   NMPDR; fig|206672.1.peg.970; -.
DR   HOGENOM; Q8G5H9; -.
DR   BioCyc; BLON206672:BL1034-MON; -.
DR   BRENDA; 1.2.1.41; 39917.
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   PANTHER; PTHR11063:SF1; GSA_DH; 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    431       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189700.
SQ   SEQUENCE   431 AA;  45571 MW;  66243B4679DABEB0 CRC64;
     MSDELSPEVF DAVCRQADQA ARAQERLAQA NTEAKNELLL AIADALDEHA ADIEAANALD
     MLESKENGMD AGKLDRLLFD VPRVAAAAQG VRHVATLPDP VGEIVRGYNL PNGLRLTQTR
     VPMGVIGMIY EARPNVTVDV ASLCLKSGNA ALLRGGHAAE RTNAATLGVI APVLEAHGFE
     SALVQSVDQY GRAGATAMME ARGHIDVLVP RGGAGLIQAV VRNSKVPVIE TGAGNVHIYI
     DKSGDLAKAI PIIINAKTQR VGVCNAAEKL LVHKDVAAEF LPQIAAALAE ANVVLQTDTT
     SYGIISGAAI EGLDLNHAAE EDWDTEYLAL KMGIKVVSDL DAAIDHINTH STGHTESIIA
     EDYAAIEEFT KRIDSAVVMV NASTRFTDGG VFGFGAELGI STQKMHARGP MGLREMTTTK
     WIGYGTGQVR A
//