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Database: UniProt/TrEMBL
Entry: C5CAZ7_MICLC
LinkDB: C5CAZ7_MICLC
Original site: C5CAZ7_MICLC 
ID   C5CAZ7_MICLC            Unreviewed;       449 AA.
AC   C5CAZ7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   19-FEB-2014, entry version 36.
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   Name=proA; OrderedLocusNames=Mlut_10150;
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC
OS   3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus
OS   lysodeikticus).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC   NCTC 2665 / VKM Ac-2230;
RX   PubMed=19948807; DOI=10.1128/JB.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F.,
RA   Dover L.G., Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N.,
RA   Lapidus A., Lowry S.R., Lykidis A., Mahillon J., Markowitz V.,
RA   Mavromatis K., Mukamolova G.V., Oren A., Rokem J.S., Smith M.C.,
RA   Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
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 (By similarity).
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; CP001628; ACS30530.1; -; Genomic_DNA.
DR   RefSeq; YP_002957084.1; NC_012803.1.
DR   ProteinModelPortal; C5CAZ7; -.
DR   STRING; 465515.Mlut_10150; -.
DR   EnsemblBacteria; ACS30530; ACS30530; Mlut_10150.
DR   GeneID; 7986741; -.
DR   KEGG; mlu:Mlut_10150; -.
DR   PATRIC; 22622672; VBIMicLut29563_0969.
DR   eggNOG; COG0014; -.
DR   HOGENOM; HOG000246356; -.
DR   KO; K00147; -.
DR   OrthoDB; EOG6FFSCX; -.
DR   BioCyc; MLUT465515:GHH6-1013-MONOMER; -.
DR   UniPathway; UPA00098; UER00360.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   HAMAP; MF_00412; ProA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR000965; G-glutamylP_reductase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   PANTHER; PTHR11063:SF1; PTHR11063:SF1; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; SSF53720; 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.
SQ   SEQUENCE   449 AA;  48005 MW;  05D385952C450CF1 CRC64;
     MQTTESTAPQ DQSGRQDAEA PRPEVEEAVR QRAEWARQAV PELAIAGRAR KDAVLRHMAE
     ALRANTAAIL TANREDRGRG REAGTSAAML DRLKLDEARV EALALALETL AGLPDPVGTV
     VRGGPLPNGV RMSQVRVPLG VVGAVYEARP NVTVDIAGIA LKSGNGVILR GGSAAESTNA
     VLIQVLREAL VDQGFDPNII QGIDDLGRPG VAALMAARGA VDVLVPRGGR ELIQRVVREA
     RVPVIETGEG NVHLYVDASA PKQMAVDIAL NSKTHRTSVC NAAETLLLHR DAEETGREVL
     RALTRAGVLL HVDEAARAWL PTLADRGDRA RDAVDATEED WGTEYLDMEM AVRVVDSLDQ
     AIEHIGRWST GHTEAIVTND LAAAERFITE VDAAAVIVNA STRFTDGGEL GLGAEVGIST
     QKMHARGPMG LEELTTTKWI LRGDGQIRR
//
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