ID   PROA_CHLTE              Reviewed;         420 AA.
AC   Q8KCE9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 42.
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=CT1473;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE006470; AAM72700.1; -; Genomic_DNA.
DR   RefSeq; NP_662358.1; -.
DR   HSSP; Q9WYC9; 1O20.
DR   GeneID; 1006019; -.
DR   GenomeReviews; AE006470_GR; CT1473.
DR   KEGG; cte:CT1473; -.
DR   NMPDR; fig|194439.1.peg.1452; -.
DR   TIGR; CT1473; -.
DR   HOGENOM; Q8KCE9; -.
DR   BioCyc; CTEP194439:CT_1473-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP 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_DHase_C.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DHase.
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    420       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189712.
SQ   SEQUENCE   420 AA;  45961 MW;  246CFED586B56A43 CRC64;
     MTEHEAIVKQ LQAVQNASRK IVPLNEETIN GLLVELADRI PAAADAILEA NRKDLERMDP
     ADPRYDRLLL NEARLNSIAT DLRNVAALPS PLHRVLEERT LPNGLELKKV SVPLGVIGII
     YESRPNVTFD VFALCLKSGN ATVLKGGSDA AYSNIAIVNL IQTVIRDRGL DPDMIYLLPA
     EREAAHILLN AVGYIDVIIP RGSQALIDFA RKHSTVPVIE TGAGIVHTYF DQSGDLAMGR
     DIVFNAKTRR PSVCNALDTL IVHESRIDDL PVLVVPLEEK NVQIFADEPA YYKLLGRYPD
     ELLEMASPEH FGTEFLSLKM SIKTVGSLEE ALNHIARHSS KHSEAIIASD QTTIDAFMKQ
     VDAAAVYANT STAFTDGAQF GLGAEIGIST QKLHARGPMA LKELCSYKWL VTGQGQVRTA
//