PROA_ECOLI
ID PROA_ECOLI Reviewed; 417 AA.
AC P07004; P77428;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 188.
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};
GN OrderedLocusNames=b0243, JW0233;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6089111; DOI=10.1093/nar/12.15.6337;
RA Deutch A.H., Rushlow K.E., Smith C.J.;
RT "Analysis of the Escherichia coli proBA locus by DNA and protein
RT sequencing.";
RL Nucleic Acids Res. 12:6337-6355(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 358-367.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 368-417.
RC STRAIN=Clinical strain;
RX PubMed=1282191; DOI=10.1111/j.1365-2958.1992.tb01788.x;
RA Lim D.;
RT "Structure and biosynthesis of unbranched multicopy single-stranded DNA by
RT reverse transcriptase in a clinical Escherichia coli isolate.";
RL Mol. Microbiol. 6:3531-3542(1992).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7034716; DOI=10.1042/bj1970269;
RA Hayzer D.J., Leisinger T.;
RT "Proline biosynthesis in Escherichia coli. Stoichiometry and end-product
RT identification of the reaction catalysed by glutamate semialdehyde
RT dehydrogenase.";
RL Biochem. J. 197:269-274(1981).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=7035170; DOI=10.1111/j.1432-1033.1982.tb05823.x;
RA Hayzer D.J., Leisinger T.;
RT "Proline biosynthesis in Escherichia coli. Purification and
RT characterisation of glutamate-semialdehyde dehydrogenase.";
RL Eur. J. Biochem. 121:561-565(1982).
RN [9]
RP SUBUNIT.
RX PubMed=6319365; DOI=10.1128/jb.157.2.545-551.1984;
RA Smith C.J., Deutch A.H., Rushlow K.E.;
RT "Purification and characteristics of a gamma-glutamyl kinase involved in
RT Escherichia coli proline biosynthesis.";
RL J. Bacteriol. 157:545-551(1984).
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, ECO:0000269|PubMed:7034716,
CC ECO:0000269|PubMed:7035170}.
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 ECO:0000269|PubMed:7034716, ECO:0000269|PubMed:7035170};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate, copper and
CC nickel ions. {ECO:0000269|PubMed:7035170}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:7035170};
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, ECO:0000269|PubMed:7035170}.
CC -!- SUBUNIT: Homodimer (Probable). May form a complex with glutamate 5-
CC kinase (proB). {ECO:0000269|PubMed:6319365, ECO:0000269|PubMed:7035170,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P07004; P0AFT5: btsR; NbExp=4; IntAct=EBI-548584, EBI-556431;
CC P07004; P16676: cysA; NbExp=3; IntAct=EBI-548584, EBI-556404;
CC P07004; P0A823: sfsA; NbExp=4; IntAct=EBI-548584, EBI-556413;
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; X00786; CAA25364.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08663.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73347.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77912.2; -; Genomic_DNA.
DR EMBL; Z12832; CAA78292.1; -; Genomic_DNA.
DR PIR; D64749; RDECER.
DR RefSeq; NP_414778.1; NC_000913.3.
DR RefSeq; WP_000893278.1; NZ_SSZK01000050.1.
DR AlphaFoldDB; P07004; -.
DR SMR; P07004; -.
DR BioGRID; 4259768; 49.
DR BioGRID; 851022; 4.
DR DIP; DIP-10568N; -.
DR IntAct; P07004; 17.
DR STRING; 511145.b0243; -.
DR SWISS-2DPAGE; P07004; -.
DR jPOST; P07004; -.
DR PaxDb; P07004; -.
DR PRIDE; P07004; -.
DR EnsemblBacteria; AAC73347; AAC73347; b0243.
DR EnsemblBacteria; BAA77912; BAA77912; BAA77912.
DR GeneID; 946680; -.
DR KEGG; ecj:JW0233; -.
DR KEGG; eco:b0243; -.
DR PATRIC; fig|1411691.4.peg.2040; -.
DR EchoBASE; EB0760; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_6; -.
DR InParanoid; P07004; -.
DR OMA; PGVCNAM; -.
DR PhylomeDB; P07004; -.
DR BioCyc; EcoCyc:GLUTSEMIALDEHYDROG-MON; -.
DR BioCyc; MetaCyc:GLUTSEMIALDEHYDROG-MON; -.
DR UniPathway; UPA00098; UER00360.
DR PRO; PR:P07004; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IMP:EcoCyc.
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 Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing; NADP;
KW Oxidoreductase; Proline biosynthesis; Reference proteome.
FT CHAIN 1..417
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189723"
FT CONFLICT 358..367
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 44630 MW; D9A4E3418EFEB488 CRC64;
MLEQMGIAAK QASYKLAQLS SREKNRVLEK IADELEAQSE IILNANAQDV ADARANGLSE
AMLDRLALTP ARLKGIADDV RQVCNLADPV GQVIDGGVLD SGLRLERRRV PLGVIGVIYE
ARPNVTVDVA SLCLKTGNAV ILRGGKETCR TNAATVAVIQ DALKSCGLPA GAVQAIDNPD
RALVSEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIYVD ESVEIAEALK
VIVNAKTQRP STCNTVETLL VNKNIADSFL PALSKQMAES GVTLHADAAA LAQLQAGPAK
VVAVKAEEYD DEFLSLDLNV KIVSDLDDAI AHIREHGTQH SDAILTRDMR NAQRFVNEVD
SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTTYKWIGI GDYTIRA
