PROA2_BACLD
ID PROA2_BACLD Reviewed; 423 AA.
AC Q65IS9; Q62U86;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Gamma-glutamyl phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GPR 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412};
GN Name=proA2 {ECO:0000255|HAMAP-Rule:MF_00412};
GN OrderedLocusNames=BLi02148, BL01984;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-
CC phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
CC {ECO:0000255|HAMAP-Rule:MF_00412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00412};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00412}.
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DR EMBL; AE017333; AAU41035.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23673.1; -; Genomic_DNA.
DR RefSeq; WP_003182464.1; NC_006322.1.
DR AlphaFoldDB; Q65IS9; -.
DR SMR; Q65IS9; -.
DR STRING; 279010.BL01984; -.
DR EnsemblBacteria; AAU23673; AAU23673; BL01984.
DR GeneID; 66215850; -.
DR KEGG; bld:BLi02148; -.
DR KEGG; bli:BL01984; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_9; -.
DR OMA; HQRGPIG; -.
DR OrthoDB; 223669at2; -.
DR BioCyc; BLIC279010:BLI_RS10630-MON; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
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; IPR020593; G-glutamylP_reductase_CS.
DR InterPro; IPR012134; Glu-5-SA_DH.
DR InterPro; IPR000965; GPR_dom.
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; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..423
FT /note="Gamma-glutamyl phosphate reductase 2"
FT /id="PRO_0000189694"
SQ SEQUENCE 423 AA; 45601 MW; 38BBCA4EA7002357 CRC64;
MTATSESISA QIEEKAIKAK TAAKSLRLAT EKEKNEALAA LADHLKQNMS YILTENAKDI
EAGRKKGYDA AYIDRLSLNE DRVLDFADGL LEVAELDDPV GETLSSWTLD NGLKAEKVSV
PLGVIGMIYE ARPNVTVDAT GLALKSGNAI VLKGGSSAIH SNTAIVSVMH QALDSTNIPR
DAVQFIESTD RSATKQLFKM KEHIDVLIPR GGGALIQEVV ENATVPVLET GVGNCHIYID
READPEKAID VMINAKTDRP AVCNALETLI VHEKWLEENS AALINALNEH GIQVHGDEKA
VQMIPGARPA GEADWQNEYL SLDLAVKVAG SLEEACDHIE TYGTKHSEAI ITENPETAKA
FLNTVDAAAL YHNASTRFTD GGALGFGAEI GISTQKLHAR GPMGLKELTT CKYIMRGDGH
IRR
