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Database: UniProt
Entry: A0A269WAW9_9BACL
LinkDB: A0A269WAW9_9BACL
Original site: A0A269WAW9_9BACL 
ID   A0A269WAW9_9BACL        Unreviewed;       280 AA.
AC   A0A269WAW9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE            Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE            Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925};
DE   AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
GN   Name=proC {ECO:0000256|HAMAP-Rule:MF_01925};
GN   ORFNames=CHH75_03135 {ECO:0000313|EMBL:PAK55267.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK55267.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK55267.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK55267.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01925};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01925}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|HAMAP-Rule:MF_01925}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAK55267.1}.
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DR   EMBL; NQLZ01000005; PAK55267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269WAW9; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000215741; Unassembled WGS sequence.
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   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   PANTHER; PTHR11645:SF51; COME OPERON PROTEIN 4; 1.
DR   PANTHER; PTHR11645; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215741}.
FT   DOMAIN          2..97
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          159..262
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   280 AA;  30517 MW;  ABCF78B64DDCFCAD CRC64;
     MKVGFIGTGS MGSLLIDSFI HLGALQPKQI LVSNRSPEKA LLLAERHPGL SVCSCNSETA
     SESDLIFLCI KPLEFKAVID EIQSSLRPEQ IAISITSPVQ LIHLESSLPC KVAKIIPSIT
     NKTGGGATLC MYGSRIKEED RQLIESLLSY ISRPVEILES HTRITSDFSS CGPAFLSLFV
     EKWIDAAVEL TGADRGTLNT LAGEMLLGTG KLLTEEGFSP EQLQERVAVP GGITAQALRL
     LNGHLNGLFY QLIQTTHDKY DEDLVKLDAA FGFTINRPRY
//
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