ID MURB_DESRM Reviewed; 303 AA. AC A4J2B3; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 1. DT 22-FEB-2023, entry version 93. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000255|HAMAP-Rule:MF_00037}; DE EC=1.3.1.98 {ECO:0000255|HAMAP-Rule:MF_00037}; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00037}; GN Name=murB {ECO:0000255|HAMAP-Rule:MF_00037}; OrderedLocusNames=Dred_0677; OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1) OS (Desulfotomaculum reducens). OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae; OC Desulforamulus. OX NCBI_TaxID=349161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.; RT "Complete sequence of Desulfotomaculum reducens MI-1."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; CC Xref=Rhea:RHEA:12248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:68483, ChEBI:CHEBI:70757; EC=1.3.1.98; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000255|HAMAP- CC Rule:MF_00037}. 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; CP000612; ABO49216.1; -; Genomic_DNA. DR RefSeq; WP_011877052.1; NC_009253.1. DR AlphaFoldDB; A4J2B3; -. DR SMR; A4J2B3; -. DR STRING; 349161.Dred_0677; -. DR EnsemblBacteria; ABO49216; ABO49216; Dred_0677. DR KEGG; drm:Dred_0677; -. DR eggNOG; COG0812; Bacteria. DR HOGENOM; CLU_035304_1_1_9; -. DR OMA; KMNAGMK; -. DR OrthoDB; 9804753at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; 1. DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; IPR016166; FAD-bd_PCMH. DR InterPro; IPR036318; FAD-bd_PCMH-like_sf. DR InterPro; IPR016167; FAD-bd_PCMH_sub1. DR InterPro; IPR016169; FAD-bd_PCMH_sub2. DR InterPro; IPR003170; MurB. DR InterPro; IPR011601; MurB_C. DR InterPro; IPR036635; MurB_C_sf. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR PANTHER; PTHR21071; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1. DR PANTHER; PTHR21071:SF4; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; KW Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..303 FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase" FT /id="PRO_1000071038" FT DOMAIN 32..212 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 176 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 226 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 296 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" SQ SEQUENCE 303 AA; 32593 MW; 07AA6525BDA3E7D3 CRC64; MIYTSLAGEL QSLVKGSIQI NEPMRKHTTW KIGGKADLFL NPSDKEDIRQ AVEFAREKAI PITVIGNGSN LLVKDGGIRG LVIKVGRGMA KITIEGTSIK AGAGALLPEL AVFACKNSLG GFGFAAGIPG SLGGAIVMNA GAMNGCVSDV LQSIVVLNER NQFEVLTKDH LNFAYRTSNL QSRGLICVET CWQGYAKDQW LIEQETKEYL AKRKAAQPQG FPNAGSVFKN PEGDFAGRLI EGCGGKGLRV GDAEVSSKHA NWILNLGRAT AQDVLILIDH LKQMVQERFG VLLQLEVKVL GED //