ID C5CAZ7_MICLC Unreviewed; 449 AA.
AC C5CAZ7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
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 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: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; Aldehyde_DH/Histidinol_DH; 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
//