ID   PROA_BACTN              Reviewed;         417 AA.
AC   Q8A1E8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 53.
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=BT_3718;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78823.1; -; Genomic_DNA.
DR   RefSeq; NP_812629.1; -.
DR   HSSP; Q9WYC9; 1O20.
DR   GeneID; 1075939; -.
DR   GenomeReviews; AE015928_GR; BT_3718.
DR   KEGG; bth:BT_3718; -.
DR   NMPDR; fig|226186.1.peg.3716; -.
DR   HOGENOM; Q8A1E8; -.
DR   OMA; Q8A1E8; QYPAACN.
DR   BioCyc; BTHE226186:BT_3718-MON; -.
DR   BRENDA; 1.2.1.41; 21018.
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; 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   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    417       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189697.
SQ   SEQUENCE   417 AA;  45645 MW;  2B2D91E6B4D7A8C5 CRC64;
     MTTNLNGTFA AVQAASRELA LLSDDTINQI LNAVADATIA ETSFILSENE KDLARMDKSN
     PKYDRLKLTE ERLKGIAADT RNVATLPSPL GRILKETSRP NGMKLTKVSV PFGVIGIIYE
     ARPNVSFDVF SLCLKSGNAC ILKGGSDADD SNRAIISVIH KVLEKFHVNP HIVELLPADR
     EATAALLNAT GYVDLIIPRG SSNLINFVRE NARIPVIETG AGICHTYFDE FGDTRKGADI
     IHNAKTRRVS VCNALDCTII HEKRLGDLPA LCDQLKESKV TIYADTQAYQ ALEGYYPAEL
     LQPATPESFG TEFLDYKMAV KTVKSFEDAL GHIQENSSRH SECIVTENKE RATLFTKIVD
     AACVYTNVST AFTDGAQFGL GAEIGISTQK LHARGPMGLE EITSYKWVIE GDGQTRW
//