ID   A0AA49QEZ8_9GAMM        Unreviewed;       245 AA.
AC   A0AA49QEZ8;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   27-MAR-2024, entry version 2.
DE   RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE            EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
DE   Flags: Fragment;
GN   Name=proA {ECO:0000313|EMBL:WLG15560.1};
OS   Pectobacterium sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=1913084 {ECO:0000313|EMBL:WLG15560.1};
RN   [1] {ECO:0000313|EMBL:WLG15560.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PS2 {ECO:0000313|EMBL:WLG15560.1};
RA   Teoh S.H.;
RT   "First Report of Pectobacterium carotovorum and Pectobacterium aroidearum
RT   Causing Bacterial Soft Rot on Curly Dwarf Pak Choy (Brassica rapa var.
RT   Chinensis) in Malaysia.";
RL   Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004985}.
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DR   EMBL; OR206484; WLG15560.1; -; mRNA.
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; 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   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650}.
FT   DOMAIN          14..140
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:WLG15560.1"
FT   NON_TER         245
FT                   /evidence="ECO:0000313|EMBL:WLG15560.1"
SQ   SEQUENCE   245 AA;  26253 MW;  D69961A0AF3F75B4 CRC64;
     ILRGGKETYR TNAATVKVIQ QALSQCGLPA AAVQAIESPD RELVNQLLKL DRYVDMLIPR
     GGAGLHKLCR EQSTIPVITG GIGVCHIYAD DSIDFDKALT VIESAKVQRP SACNSLETLL
     VNQHIADRFL PALSKKMAAA GVTLHASPSA MPYLTDGPAS VVAVEEANYN DEWLSNDLNV
     TLVDDLDAAV AHIREHGTQH SDAILTRSLS NAERFVREVD SSAVYVNAST RFTDGGQFGL
     GAEVA
//