P5CR_SHIFL
ID P5CR_SHIFL Reviewed; 269 AA.
AC P0A9L9; P00373;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=SF0322, S0330;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41981.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15859.1; -; Genomic_DNA.
DR RefSeq; NP_706274.1; NC_004337.2.
DR RefSeq; WP_001295331.1; NZ_WPGW01000023.1.
DR AlphaFoldDB; P0A9L9; -.
DR SMR; P0A9L9; -.
DR STRING; 198214.SF0322; -.
DR EnsemblBacteria; AAN41981; AAN41981; SF0322.
DR EnsemblBacteria; AAP15859; AAP15859; S0330.
DR GeneID; 1027435; -.
DR GeneID; 66671315; -.
DR KEGG; sfl:SF0322; -.
DR KEGG; sfx:S0330; -.
DR PATRIC; fig|198214.7.peg.370; -.
DR HOGENOM; CLU_042344_3_1_6; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 1349288at2; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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..269
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187297"
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
