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 06-MAR-2013, entry version 44. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase; DE EC=1.1.1.158; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase; GN Name=murB; OrderedLocusNames=BPUM_1416; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; 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., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., 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 (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the MurB family. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. 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; YP_001486659.1; NC_009848.1. DR ProteinModelPortal; A8FCY2; -. DR STRING; A8FCY2; -. DR EnsemblBacteria; EBBACT00000065134; EBBACP00000063467; EBBACG00000065125. DR GeneID; 5620683; -. DR GenomeReviews; CP000813_GR; BPUM_1416. DR KEGG; bpu:BPUM_1416; -. DR PATRIC; 18966667; VBIBacPum16546_1430. DR eggNOG; COG0812; -. DR HOGENOM; HOG000284355; -. DR KO; K00075; -. DR OMA; CAGSIFR; -. DR ProtClustDB; PRK13905; -. DR BioCyc; BPUM315750:GH6N-1505-MONOMER; -. DR UniPathway; UPA00219; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; -; 1. DR HAMAP; MF_00037; MurB; 1; -. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR003170; MurB. DR InterPro; IPR011601; MurB_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR PANTHER; PTHR21071; PTHR21071; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; FAD-binding_2; 1. DR SUPFAM; SSF56194; MurB_C; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD; KW Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis. FT CHAIN 1 303 UDP-N-acetylenolpyruvoylglucosamine FT reductase. FT /FTId=PRO_1000057272. FT DOMAIN 30 196 FAD-binding PCMH-type. FT ACT_SITE 174 174 By similarity. FT ACT_SITE 225 225 Proton donor (By similarity). FT ACT_SITE 295 295 By similarity. 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 //