ID MURB_PHEZH Reviewed; 300 AA. AC B4RFG1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 28-JUN-2011, entry version 24. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase; DE EC=1.1.1.158; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase; GN Name=murB; OrderedLocusNames=PHZ_c2321; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., RA Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). CC -!- FUNCTION: Cell wall formation (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl- CC 3-O-(1-carboxyvinyl)-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; CP000747; ACG78731.1; -; Genomic_DNA. DR RefSeq; YP_002131160.1; NC_011144.1. DR GeneID; 6791842; -. DR GenomeReviews; CP000747_GR; PHZ_c2321. DR KEGG; pzu:PHZ_c2321; -. DR HOGENOM; HBG686573; -. DR OMA; SKKHAGF; -. DR ProtClustDB; PRK13905; -. 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:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 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 Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1. DR Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1. DR Gene3D; G3DSA:3.90.78.10; MurB_C; 1. DR PANTHER; PTHR21071; MurB; 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 1 300 UDP-N-acetylenolpyruvoylglucosamine FT reductase. FT /FTId=PRO_1000191438. FT DOMAIN 27 216 FAD-binding PCMH-type. FT ACT_SITE 172 172 By similarity. FT ACT_SITE 223 223 Proton donor (By similarity). FT ACT_SITE 293 293 By similarity. SQ SEQUENCE 300 AA; 32008 MW; 61251C19CB0731BB CRC64; MTWKDRLPAV RGKLLRDEPL APFTWFRVGG PADVIFLPED EDDLAAFLKA LPAEVPVTVL GVGSNTLVRD GGVDGVVIRL GKAFAKVEPR GEGRLYAGAA ALDAVVAREA GKAGIAGLEF YRGVPGTIGG ALVMNAGCYG AETKDVLVEA YALTRAGERL TLSNADLGYS YRKSARAAAE PLIFLGALFE GRPDDPAAIE ARMAEITERR EKTQPIREKT GGSTFKNPPG HSSWKLVDEA GWRGKLFGGA MFSPLHSNFL INTGEATAAD LEGLGEAVRA DVKAKFGVDL DWEIKRIGRP //