ID W4AG56_9BACL Unreviewed; 280 AA.
AC W4AG56;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=C169_28495 {ECO:0000313|EMBL:ETT30374.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT30374.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT30374.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT30374.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT30374.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASPT01000075; ETT30374.1; -; Genomic_DNA.
DR RefSeq; WP_036644497.1; NZ_ASPT01000075.1.
DR AlphaFoldDB; W4AG56; -.
DR PATRIC; fig|1227076.4.peg.5876; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000019053; 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}.
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; 30699 MW; 83D932FD3CD914FC CRC64;
MKVGFIGTGS MGSLLIEAFI QSGALLPEQI RVSNRSPEKA QKLAKRHPGL TVCSSNTETA
SQSDLFFLCV KPLEFKTVIS EIKDQLEARQ IAISITSPVQ LIHLESTLPC KVAKIIPSIT
NITGGGASLC MYGSRIKEED RQLIESLLSY ISRPLEILES HTRITSDFSS CGPAFLSLFM
EKWIDAAVEM TGIDRKTLNA LAGEMLLGTG KLLTEEGFSP EQLQERVAVP GGITAQALTL
LESNLNGLFY QLIQTTHDKY EEDLAKLDAA FGFTINRPRY
//
