ID A0A7Z2K699_9BACI Unreviewed; 278 AA. AC A0A7Z2K699; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 08-NOV-2023, entry version 7. 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=GNK04_15175 {ECO:0000313|EMBL:QHA92661.1}; OS Bacillus sp. N1-1. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2682541 {ECO:0000313|EMBL:QHA92661.1, ECO:0000313|Proteomes:UP000441258}; RN [1] {ECO:0000313|EMBL:QHA92661.1, ECO:0000313|Proteomes:UP000441258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N1-1 {ECO:0000313|EMBL:QHA92661.1, RC ECO:0000313|Proteomes:UP000441258}; RA Qu C.; RL Submitted (DEC-2019) 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 --------------------------------------------------------------------------- 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; CP046564; QHA92661.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Z2K699; -. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000441258; 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 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 163..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" SQ SEQUENCE 278 AA; 30757 MW; 52B77D20B140DD0E CRC64; MKIGVIGTGN MGTILVSSFI DSCAVIPSHL TIVNRSSEKA SKLKQQYPSL NVVKSADEVV KKSDMIFICV KPHEYFPLFK KIRSNLKQQQ LIVSITSPIK VSEIESFVTC DVARAIPSIT NRALSGASLV TFGSRCSEAN KVKLLYLMSQ ISTPIETDED ITRVSSDIVS CGPAFLSYLI QQFIEGAVTE TNISNEQATI LATEMLIGMG KLLEKDYFSL ETLQRKVTVK GGVTGEGLKV LEAETGEMFH HLIQSTHRKF KEDREGIKVQ FKEESKQK //