ID P5CR_ECOLI Reviewed; 269 AA.
AC P0A9L8; P00373; Q2MC39;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925};
GN OrderedLocusNames=b0386, JW0377;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=6296787; DOI=10.1093/nar/10.23.7701;
RA Deutch A.H., Smith C.J., Rushlow K.E., Kretschmer P.J.;
RT "Escherichia coli delta 1-pyrroline-5-carboxylate reductase: gene sequence,
RT protein overproduction and purification.";
RL Nucleic Acids Res. 10:7701-7714(1982).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=12133; DOI=10.1128/jb.129.1.108-114.1977;
RA Rossi J.J., Vender J., Berg C.M., Coleman W.H.;
RT "Partial purification and some properties of delta1-pyrroline-5-carboxylate
RT reductase from Escherichia coli.";
RL J. Bacteriol. 129:108-114(1977).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. Does not catalyze the reverse reaction. {ECO:0000255|HAMAP-
CC Rule:MF_01925, ECO:0000269|PubMed:12133, ECO:0000269|PubMed:6296787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000269|PubMed:12133,
CC ECO:0000269|PubMed:6296787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000269|PubMed:12133,
CC ECO:0000269|PubMed:6296787};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate.
CC {ECO:0000269|PubMed:12133}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01925, ECO:0000269|PubMed:12133, ECO:0000269|PubMed:6296787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925,
CC ECO:0000269|PubMed:6296787}.
CC -!- MISCELLANEOUS: Can use either NADPH or NADH, but the activity observed
CC with NADPH is severalfold greater. {ECO:0000305|PubMed:12133}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR EMBL; J01665; AAA86433.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18110.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73489.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76167.1; -; Genomic_DNA.
DR PIR; A00385; RDECC.
DR RefSeq; NP_414920.1; NC_000913.3.
DR RefSeq; WP_001295331.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0A9L8; -.
DR SMR; P0A9L8; -.
DR BioGRID; 4263533; 36.
DR BioGRID; 849425; 1.
DR DIP; DIP-47863N; -.
DR IntAct; P0A9L8; 4.
DR STRING; 511145.b0386; -.
DR jPOST; P0A9L8; -.
DR PaxDb; 511145-b0386; -.
DR EnsemblBacteria; AAC73489; AAC73489; b0386.
DR GeneID; 75202809; -.
DR GeneID; 945034; -.
DR KEGG; ecj:JW0377; -.
DR KEGG; eco:b0386; -.
DR PATRIC; fig|1411691.4.peg.1892; -.
DR EchoBASE; EB0762; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_3_1_6; -.
DR InParanoid; P0A9L8; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 9805754at2; -.
DR PhylomeDB; P0A9L8; -.
DR BioCyc; EcoCyc:PYRROLINECARBREDUCT-MONOMER; -.
DR BioCyc; MetaCyc:PYRROLINECARBREDUCT-MONOMER; -.
DR UniPathway; UPA00098; UER00361.
DR PRO; PR:P0A9L8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IDA:EcoCyc.
DR GO; GO:0055129; P:L-proline biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR NCBIfam; TIGR00112; proC; 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00521; P5CR; 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..269
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187289"
SQ SEQUENCE 269 AA; 28145 MW; C5E2CED36BCC508D CRC64;
MEKKIGFIGC GNMGKAILGG LIASGQVLPG QIWVYTPSPD KVAALHDQFG INAAESAQEV
AQIADIIFAA VKPGIMIKVL SEITSSLNKD SLVVSIAAGV TLDQLARALG HDRKIIRAMP
NTPALVNAGM TSVTPNALVT PEDTADVLNI FRCFGEAEVI AEPMIHPVVG VSGSSPAYVF
MFIEAMADAA VLGGMPRAQA YKFAAQAVMG SAKMVLETGE HPGALKDMVC SPGGTTIEAV
RVLEEKGFRA AVIEAMTKCM EKSEKLSKS
//
