ID A0A4Y3H2Z1_9BIFI Unreviewed; 266 AA. AC A0A4Y3H2Z1; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 27-MAR-2024, entry version 15. 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 ECO:0000313|EMBL:RHJ80967.1}; GN ORFNames=DW102_05175 {ECO:0000313|EMBL:RHJ80967.1}; OS Bifidobacterium pseudocatenulatum. OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=28026 {ECO:0000313|EMBL:RHJ80967.1, ECO:0000313|Proteomes:UP000286301}; RN [1] {ECO:0000313|EMBL:RHJ80967.1, ECO:0000313|Proteomes:UP000286301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM08-25 {ECO:0000313|EMBL:RHJ80967.1, RC ECO:0000313|Proteomes:UP000286301}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) 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:RHJ80967.1}. 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; QRMQ01000004; RHJ80967.1; -; Genomic_DNA. DR RefSeq; WP_034880672.1; NZ_QRMR01000004.1. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000286301; 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 NCBIfam; TIGR00112; proC; 1. DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1. DR PANTHER; PTHR11645:SF0; 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. 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|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01925}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925, KW ECO:0000313|EMBL:RHJ80967.1}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}. FT DOMAIN 5..101 FT /note="Pyrroline-5-carboxylate reductase catalytic N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF03807" FT DOMAIN 169..264 FT /note="Pyrroline-5-carboxylate reductase dimerisation" FT /evidence="ECO:0000259|Pfam:PF14748" FT BINDING 9..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1" FT BINDING 71..74 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1" SQ SEQUENCE 266 AA; 27791 MW; 19700ADA382F0D8C CRC64; MANPTIGFIG YGNMAQAIAE GLVNAGTISG DDIVACAAHY DKLERNAAKL GAKAVHTAAQ VAEVADVVVI AIKPYQIEAV ISPIVDQLAQ PNTIVVSIAA GWDLNKFRDL FGTSFEQAHI QCTIPNTPMA VGKGVLVTEI DNTLTQEQTE TFESLFSSIS LIERVDTAHM GIGMCIAGCA PAFTDMYIEA LGDAGVKYGL QRATAYRLAA KMVEGVGALY LANETHPGAM KDAVCSPGGT TIRGVASLEE SAFRGAVIKA VDAIEA //