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Database: UniProt
Entry: A0A1E3T5P8_9MYCO
LinkDB: A0A1E3T5P8_9MYCO
Original site: A0A1E3T5P8_9MYCO 
ID   A0A1E3T5P8_9MYCO        Unreviewed;       419 AA.
AC   A0A1E3T5P8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000256|HAMAP-Rule:MF_00412};
GN   ORFNames=BHQ21_03810 {ECO:0000313|EMBL:ODR09789.1};
OS   Mycobacterium sherrisii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR09789.1, ECO:0000313|Proteomes:UP000094224};
RN   [1] {ECO:0000313|Proteomes:UP000094224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000979, ECO:0000256|HAMAP-
CC         Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODR09789.1}.
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DR   EMBL; MIHC01000004; ODR09789.1; -; Genomic_DNA.
DR   RefSeq; WP_069399040.1; NZ_MIHC01000004.1.
DR   AlphaFoldDB; A0A1E3T5P8; -.
DR   STRING; 243061.AWC25_15200; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000094224; Unassembled WGS sequence.
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   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   NCBIfam; TIGR00407; proA; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00412};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW   Rule:MF_00412}; Reference proteome {ECO:0000313|Proteomes:UP000094224}.
FT   DOMAIN          13..292
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   419 AA;  43742 MW;  C8EDE060E2BE2FD0 CRC64;
     MSLQAPSRPD LRQEVHAAAR RARIASRALA LLPTVAKDQA LHSAANAITA NTRQILAANA
     DDLDAARAAG TSDAMLDRLA LDATRVDGIA AGLRQVAGLP DPIGEVLRGY TLPNGLQLRQ
     QRVPLGVVGM IYEGRPNVTV DAFGLALKSG NAVLLRGSSS AARSNQALVE VLRSSLASED
     LPADAVQLLC ADDRSTVTHL IQARGLVDVV IPRGGASLIE AVVRDAQVPT IETGVGNCHV
     YVDGGADLDV AERILLNSKT RRPSVCNAAE TLLVDRAIAA HAVPRLVAAL QDAGVTVHGG
     LLEAPSEDDL RREYLSMDIA VTVVDGVDAA IAHINEYGTG HTEAIVTDNM AAAQRFTDGV
     DAAAVMVNAS TGFTDGEQFG FGAEIGISTQ KLHARGPMGL PELTSTKWIA WGDGQVRPA
//
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