ID MURB_BURP1 Reviewed; 349 AA. AC Q3JVB9; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 29-MAY-2024, entry version 100. 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}; GN OrderedLocusNames=BURPS1710b_1072; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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; CP000124; ABA49889.1; -; Genomic_DNA. DR RefSeq; WP_009929228.1; NC_007434.1. DR AlphaFoldDB; Q3JVB9; -. DR SMR; Q3JVB9; -. DR EnsemblBacteria; ABA49889; ABA49889; BURPS1710b_1072. DR KEGG; bpm:BURPS1710b_1072; -. DR HOGENOM; CLU_035304_0_0_4; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002700; Chromosome I. 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: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 NCBIfam; TIGR00179; murB; 1. 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 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..349 FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase" FT /id="PRO_0000224672" FT DOMAIN 26..197 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 173 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 249 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 345 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" SQ SEQUENCE 349 AA; 37588 MW; 20ECA1AE49550D70 CRC64; MPMSRPDSAV SLLPDYSLRA HNTFGFDARA RVAARIGSPG QFASLARDPR VAGLDRLVLG GGSNVVFTRD FDGLVLLDEI RGRALVREDD GAWYVEAGGG ENWHAFVEWT LAEGMPGLEN LALIPGTVGA APIQNIGAYG LEMKEHFASL RAVELATGEL VEFDAARCAF GYRDSFFKRD GRGRFAIVAV TFRLPKAWTP RIGYADVARE LAARGIDARA VRARDVFDAV VAIRRAKLPD PLALGNAGSF FKNPVIDAQA FAALRAREPD IVSYPQPDGR VKLAAGWLID RCGWKGRALG AAAVHERQAL VLVNLGGASG ADVLALAHAI RRDVLGRFGV ELEMEPVCL //