PROA_THET2
ID PROA_THET2 Reviewed; 413 AA.
AC P54903;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 25-MAY-2022, entry version 138.
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=TT_C1564;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7988899; DOI=10.1111/j.1574-6968.1994.tb07201.x;
RA Kosuge T., Tabata K., Hoshino T.;
RT "Molecular cloning and sequence analysis of the proBA operon from an
RT extremely thermophilic eubacterium Thermus thermophilus.";
RL FEMS Microbiol. Lett. 123:55-61(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06238.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D29973; BAA06238.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE017221; AAS81906.1; -; Genomic_DNA.
DR RefSeq; WP_011173936.1; NC_005835.1.
DR AlphaFoldDB; P54903; -.
DR SMR; P54903; -.
DR STRING; 262724.TT_C1564; -.
DR EnsemblBacteria; AAS81906; AAS81906; TT_C1564.
DR KEGG; tth:TT_C1564; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_0; -.
DR OMA; PGVCNAM; -.
DR OrthoDB; 223669at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000592; 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.
FT CHAIN 1..413
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189803"
SQ SEQUENCE 413 AA; 45851 MW; EC63FDFF0FC2B71E CRC64;
MTATSLWELA ERARKRLSEI AKGNRDRALL AMADLLEARW EEVLRANRED LEEAERTGLP
KAKLDRLALK EKDLKTLTEG LRQIARLPDP LGRIEGLAKR PNGLRVGRMR VPLGLIGFIY
EARPGATVEA VSVALKAGNA MLLRGGKEAF RSNRALVALW HEALEEAGLP EEAVTLVPTT
DREAVLEMCR LELLDLLIPR GGEELIRLVQ QEARVPVLAH AKGVNHLYVD EKADLSMALR
LALNGKTQRP AVCNALEAVL VHEKVAEAFL PRLEKAMREK GVELRACPRA LPLLKEAVPA
REDEWDREYL DLVLRVKVVS GLEEALAHIA RYGSRHTEAI CTEDPKAAWR FLEEVDASLV
LWNASTRFND GFELGLGAEI GISTSKLHAY GPMGPLELTT LKWVALGEGQ ERT
