ID A0A5B3GSG5_9BACT Unreviewed; 260 AA. AC A0A5B3GSG5; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-NOV-2024, entry version 13. DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|NCBIfam:TIGR00112}; 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, ECO:0000256|NCBIfam:TIGR00112}; DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925}; GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925, GN ECO:0000313|EMBL:KAA2376477.1}; GN ORFNames=F2Y10_12745 {ECO:0000313|EMBL:KAA2376477.1}; OS Alistipes onderdonkii. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=328813 {ECO:0000313|EMBL:KAA2376477.1, ECO:0000313|Proteomes:UP000322940}; RN [1] {ECO:0000313|EMBL:KAA2376477.1, ECO:0000313|Proteomes:UP000322940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIOML-A266 {ECO:0000313|EMBL:KAA2376477.1, RC ECO:0000313|Proteomes:UP000322940}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). 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 + NADH + 2 CC H(+); 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 + NADPH + 2 CC H(+); 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:KAA2376477.1}. 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; VVXH01000015; KAA2376477.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5B3GSG5; -. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000322940; 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 FunFam; 1.10.3730.10:FF:000001; Pyrroline-5-carboxylate reductase; 1. 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:KAA2376477.1}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..260 FT /note="Pyrroline-5-carboxylate reductase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5024357232" FT DOMAIN 2..96 FT /note="Pyrroline-5-carboxylate reductase catalytic N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF03807" FT DOMAIN 161..259 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 68..71 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1" SQ SEQUENCE 260 AA; 26851 MW; 96726C233FF849A7 CRC64; MKVGFIGFGN MAQALAAGLA ASGALQPGQI GACARDRAKL HRNTKPHGFL AFDDAAGVAG FADVVVVAVK PYQVEAVLAP VKGMLAGKVV VSVAAGMTFD RYEEILAPGT HHLSTIPNTP VAVCEGIVVC ERRHSLSEAE WQSVQALLSH VGLVVTVDTA QLGIAGTVCG CGPAFVAMFI EALADAAVKH GIVRADAYRM ASQMVVGTGK LQLATGQHPA VMKDAVCSPG GTTIVGVAEL ERKRFRGAVI DAIDAIQDKK //