ID A0A4Y3H2Z1_9BIFI Unreviewed; 266 AA. AC A0A4Y3H2Z1; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 16-OCT-2019, entry version 2. 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:GEA41134.1}; GN ORFNames=DN0207_11160 {ECO:0000313|EMBL:GEA41134.1}; OS Bifidobacterium pseudocatenulatum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=28026 {ECO:0000313|EMBL:GEA41134.1}; RN [1] {ECO:0000313|EMBL:GEA41134.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 113353 {ECO:0000313|EMBL:GEA41134.1}; RA Miura T., Furukawa M., Shimamura M., Ohyama Y., Yamazoe A., RA Kawasaki H.; RT "Draft genome sequence of Bifidobacterium pseudocatenulatum NBRC RT 113353."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate CC (PCA) to 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, CC ChEBI:CHEBI:15893, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP- CC 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, CC ChEBI:CHEBI:15893, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01925}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GEA41134.1}. 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; BJLC01000001; GEA41134.1; -; Genomic_DNA. DR RefSeq; WP_034880672.1; NZ_QRMR01000004.1. DR UniPathway; UPA00098; UER00361. 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 Pfam; PF03807; F420_oxidored; 1. DR Pfam; PF14748; P5CR_dimer; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00112; proC; 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}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}. FT DOMAIN 5 101 F420_oxidored. {ECO:0000259|Pfam: FT PF03807}. FT DOMAIN 169 264 P5CR_dimer. {ECO:0000259|Pfam:PF14748}. 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 //