ID   P5CR1_BACSH             Reviewed;         297 AA.
AC   E0TY11; O07508; O31828; P14383;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5C reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5CR 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE   AltName: Full=PCA reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
GN   Name=proH; OrderedLocusNames=BSUW23_09835;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-257.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=1849493; DOI=10.1016/0378-1119(91)90111-n;
RA   Ahn K.S., Wake R.G.;
RT   "Variations and coding features of the sequence spanning the replication
RT   terminus of Bacillus subtilis 168 and W23 chromosomes.";
RL   Gene 98:107-112(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=2493444; DOI=10.1128/jb.171.3.1402-1408.1989;
RA   Lewis P.J., Wake R.G.;
RT   "DNA and protein sequence conservation at the replication terminus in
RT   Bacillus subtilis 168 and W23.";
RL   J. Bacteriol. 171:1402-1408(1989).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADM38011.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP002183; ADM38011.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M24523; AAA22722.1; -; Genomic_DNA.
DR   PIR; E69682; E69682.
DR   AlphaFoldDB; E0TY11; -.
DR   SMR; E0TY11; -.
DR   EnsemblBacteria; ADM38011; ADM38011; BSUW23_09835.
DR   KEGG; bss:BSUW23_09835; -.
DR   HOGENOM; CLU_042344_0_1_9; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000002233; 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.
FT   CHAIN           1..297
FT                   /note="Pyrroline-5-carboxylate reductase 1"
FT                   /id="PRO_0000403662"
SQ   SEQUENCE   297 AA;  31924 MW;  C98FE22530CE41AD CRC64;
     MRTKKRTKEM LPIFDQKKVA FIGAGSMAEG MISGIVRANK IPKQNICVTN RSNTERLAEL
     ELQYGIKGAS PNQICIEDMD VLILAMKPKD AESALSSLKT RIQPHQLILS VLAGITTSFI
     EQSLLNQQPV VRVMPNTSSM IGASATAIAL GKYVSEDLQK LAEALLGCMG EVYTIQENQM
     DIFTGIAGSG PAYFYYLMEF IEKTGEEAGL DKQLSRSIGA QTLLGAAKML METGEQPEVL
     RDNITSPNGT TAAGLQALKK SGGGEAISQA IKHAAKRSKE ISDDIEKTAA PLSGVIK