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P5CR_HELPY
ID   P5CR_HELPY              Reviewed;         257 AA.
AC   O25773;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 127.
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}; OrderedLocusNames=HP_1158;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000255|HAMAP-Rule:MF_01925}.
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};
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};
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR   EMBL; AE000511; AAD08197.1; -; Genomic_DNA.
DR   PIR; F64664; F64664.
DR   RefSeq; NP_207949.1; NC_000915.1.
DR   RefSeq; WP_000404448.1; NC_018939.1.
DR   AlphaFoldDB; O25773; -.
DR   SMR; O25773; -.
DR   DIP; DIP-3659N; -.
DR   IntAct; O25773; 4.
DR   MINT; O25773; -.
DR   STRING; 85962.C694_05980; -.
DR   PaxDb; O25773; -.
DR   EnsemblBacteria; AAD08197; AAD08197; HP_1158.
DR   KEGG; hpy:HP_1158; -.
DR   PATRIC; fig|85962.47.peg.1242; -.
DR   eggNOG; COG0345; Bacteria.
DR   OMA; EQICTPK; -.
DR   PhylomeDB; O25773; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..257
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000187291"
SQ   SEQUENCE   257 AA;  28162 MW;  62F390B35EE5D23D CRC64;
     MEILQFIGYG NMAQAILEGA HEILSKRFIL EITGRNPEKI APFLQEKNIQ AQIVPYKDAI
     DIHQKFVFLL FKPYNLKDFN YQGQAKSVLS ALAGVGFKAL SDAIDSLHYL KCMPNIASKF
     ALSSTAVCEK SPMPLISQKA LSVIESFGNC VRVGHEELVD ASVATNGSAL AFLSLVANSL
     KDAGIREGLN ARGSLELVKM SFKGFAKLLE KERPEMIIEQ ICTPKGATIE GLSVLEKKGV
     RGAFIEACHK SVKKMRL
 
 
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