PROA_MYCBP
ID PROA_MYCBP Reviewed; 415 AA.
AC A1KLC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GPR {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 {ECO:0000255|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=BCG_2444c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL72432.1; -; Genomic_DNA.
DR RefSeq; WP_003412516.1; NC_008769.1.
DR AlphaFoldDB; A1KLC0; -.
DR SMR; A1KLC0; -.
DR GeneID; 45426416; -.
DR KEGG; mbb:BCG_2444c; -.
DR HOGENOM; CLU_030231_0_0_11; -.
DR OMA; PGVCNAM; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000001472; 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; 2.
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.
FT CHAIN 1..415
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_1000049964"
SQ SEQUENCE 415 AA; 43745 MW; 071C9872F8C9A8AC CRC64;
MTVPAPSQLD LRQEVHDAAR RARVAARRLA SLPTTVKDRA LHAAADELLA HRDQILAANA
EDLNAAREAD TPAAMLDRLS LNPQRVDGIA AGLRQVAGLR DPVGEVLRGY TLPNGLQLRQ
QRVPLGVVGM IYEGRPNVTV DAFGLTLKSG NAALLRGSSS AAKSNEALVA VLRTALVGLE
LPADAVQLLS AADRATVTHL IQARGLVDVV IPRGGAGLIE AVVRDAQVPT IETGVGNCHV
YVHQAADLDV AERILLNSKT RRPSVCNAAE TLLVDAAIAE TALPRLLAAL QHAGVTVHLD
PDEADLRREY LSLDIAVAVV DGVDAAIAHI NEYGTGHTEA IVTTNLDAAQ RFTEQIDAAA
VMVNASTAFT DGEQFGFGAE IGISTQKLHA RGPMGLPELT STKWIAWGAG HTRPA
