PROA_CAMJE
ID PROA_CAMJE Reviewed; 410 AA.
AC P53000; Q0PAV8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=Cj0558c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=8341262; DOI=10.1007/bf00276880;
RA Louie H., Chan V.L.;
RT "Cloning and characterization of the gamma-glutamyl phosphate reductase
RT gene of Campylobacter jejuni.";
RL Mol. Gen. Genet. 240:29-35(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; M74579; AAA23030.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34704.1; -; Genomic_DNA.
DR PIR; F81402; F81402.
DR PIR; S35213; S35213.
DR RefSeq; WP_002858629.1; NC_002163.1.
DR RefSeq; YP_002343989.1; NC_002163.1.
DR AlphaFoldDB; P53000; -.
DR SMR; P53000; -.
DR STRING; 192222.Cj0558c; -.
DR PaxDb; P53000; -.
DR PRIDE; P53000; -.
DR EnsemblBacteria; CAL34704; CAL34704; Cj0558c.
DR GeneID; 904885; -.
DR KEGG; cje:Cj0558c; -.
DR PATRIC; fig|192222.6.peg.550; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_7; -.
DR OMA; PGVCNAM; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000799; 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; Reference proteome.
FT CHAIN 1..410
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189710"
FT CONFLICT 57
FT /note="A -> K (in Ref. 1; AAA23030)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="S -> N (in Ref. 1; AAA23030)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="M -> I (in Ref. 1; AAA23030)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> T (in Ref. 1; AAA23030)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="K -> E (in Ref. 1; AAA23030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46000 MW; EB27A90652906668 CRC64;
MRNLLENIKK NSQKLLNLTP KDKEKIILKL AQILRENFKI ILEANKKDMA NFTKSGAMKD
RLLLDEKRIL ALCEGLEKIA YIEDPIGKIS KGWKNYAGLS IQKMSIPLGL ICVIYEARPS
LSAEIAALMI KSSNACVFKG GSEAKFTNEA IFTLVNKVLK EFDLQDCFAM FTQRDEILQI
LAFDDLIDVI IPRGSSNMIQ EIANNTKIPL IKQNKGLCHA FVDQSANLDM ALKIILNAKC
QRVSVCNALE TLLIHEKIAK NFISLLIPEF EKFKVKIHAH ENALAYFNNS NLKIFKANEN
TFDTEWLDFA LSVKLVKDCD EAIEHINKHS SLHSETIISN DASNIAKFQR LINSSCIYAN
ASTRFSDGGE FGFGGEVGIS TSKLHARGPM GIEDICTYKY IINGEGQIRE
