ID MURB_BACP2 Reviewed; 303 AA. AC A8FCY2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-NOV-2024, entry version 99. 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=BPUM_1416; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3-O-(1- CC carboxyvinyl)-alpha-D-glucosamine + NADPH + H(+); 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; CP000813; ABV62099.1; -; Genomic_DNA. DR RefSeq; WP_012009870.1; NZ_VEIS01000003.1. DR AlphaFoldDB; A8FCY2; -. DR SMR; A8FCY2; -. DR STRING; 315750.BPUM_1416; -. DR KEGG; bpu:BPUM_1416; -. DR eggNOG; COG0812; Bacteria. DR HOGENOM; CLU_035304_1_1_9; -. DR OrthoDB; 9804753at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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: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 NCBIfam; TIGR00179; murB; 1. DR PANTHER; PTHR21071; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1. DR PANTHER; PTHR21071:SF5; 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 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. FT CHAIN 1..303 FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase" FT /id="PRO_1000057272" FT DOMAIN 30..196 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 174 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 225 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 295 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" SQ SEQUENCE 303 AA; 33353 MW; DF29FD0990A96454 CRC64; MENLKNELLE AQVGKVLENE PLANHTTMKI GGPADLLIIP KDIDAVKTIM DHVKKHQTNW TVIGRGSNLL VLDKGIRGVV LKLGTGLDHL TVNDEEITVG GGYSVVRLAT SLSKQGLSGL EFAAGIPGSI GGAVYMNAGA HGSDISKILV KARILFEDGS IEWLTNEQMN FSYRTSVLQK ERPGIVLEAV FKLKQDDREK ITKKMQQNKD YRKETQPYNR PCAGSIFRNP LPEYAGQLVE KANLKGYQLG GARISDMHGN FIVNAGGATA QDVLDLIQFI QKKIKEDYNV EMHTEVEIIG EEN //