PROA_BURTA
ID PROA_BURTA Reviewed; 423 AA.
AC Q2SZ88;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BTH_I1214;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC38329.1; -; Genomic_DNA.
DR PDB; 4GHK; X-ray; 2.25 A; A/B/C/D=1-423.
DR PDBsum; 4GHK; -.
DR AlphaFoldDB; Q2SZ88; -.
DR SMR; Q2SZ88; -.
DR PRIDE; Q2SZ88; -.
DR EnsemblBacteria; ABC38329; ABC38329; BTH_I1214.
DR KEGG; bte:BTH_I1214; -.
DR HOGENOM; CLU_030231_0_0_4; -.
DR OMA; PGVCNAM; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000001930; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis.
FT CHAIN 1..423
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000252566"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 26..42
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:4GHK"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:4GHK"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4GHK"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:4GHK"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:4GHK"
SQ SEQUENCE 423 AA; 45309 MW; BFC044A712674A8C CRC64;
MDIDQYMTDV GRRARRASRS IARASTAAKN AALEAVARAI ERDAGALKAA NARDVARAKD
KGLDAAFVDR LTLSDKALKT MVEGLRQVAT LPDPIGEMSN LKYRPSGIQV GQMRVPLGVI
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLAE AGLPQDTVQV
VETADRAAVG RLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRASV
TKALTVCDNA KTHRYGTCNT METLLVARGI APAVLSPLGR LYREKGVELR VDADARAVLE
AAGVGPLVDA TDEDWRTEYL APVLAIKIVD GIDAAIEHIN EYGSHHTDAI VTEDHDRAMR
FLREVDSASV MVNASTRFAD GFEFGLGAEI GISNDKLHAR GPVGLEGLTS LKYVVLGHGE
GRQ
