ID E0RCE4_PAEP6 Unreviewed; 288 AA.
AC E0RCE4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=PPE_02688 {ECO:0000313|EMBL:ADM70516.1};
OS Paenibacillus polymyxa (strain E681).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70516.1, ECO:0000313|Proteomes:UP000002227};
RN [1] {ECO:0000313|EMBL:ADM70516.1, ECO:0000313|Proteomes:UP000002227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E681 {ECO:0000313|EMBL:ADM70516.1,
RC ECO:0000313|Proteomes:UP000002227};
RX PubMed=20851896; DOI=10.1128/JB.00983-10;
RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT Paenibacillus polymyxa E681.";
RL J. Bacteriol. 192:6103-6104(2010).
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}.
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DR EMBL; CP000154; ADM70516.1; -; Genomic_DNA.
DR RefSeq; WP_013310664.1; NZ_CP048794.1.
DR AlphaFoldDB; E0RCE4; -.
DR KEGG; ppy:PPE_02688; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_0_1_9; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000002227; 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 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 NCBIfam; TIGR00112; proC; 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF49; PYRROLINE-5-CARBOXYLATE REDUCTASE 1; 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.
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 ECO:0000313|EMBL:ADM70516.1};
KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}.
FT DOMAIN 13..112
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 175..279
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 83..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 288 AA; 30964 MW; A69C602164881D44 CRC64;
MCESQTKVLI NEQITFFGAG SMAEAIIRGM TARSVVKPSG ITVINRSNQA RLEELQKQYG
VLFQTEDAAK TELLRRSPVI VLAMKPKDAA QALGQLGPLL SDEQLIISVI AGLSIRTMQT
LLGRKQPIAR TMPNTSSSIG LGATGISFSK EISENQRKNV LTMFESVGTV TVIEEEKMDV
LTGISGSGPA YVYYLMEAMI AGGIRGGLTP EQAHELTVQT ALGAARMVQQ TGEEPSALRH
KIMSPNGSTV AALETLDKGD FYETVIAAVQ RCAERSREMG AVLKEGNE
//
