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 02-DEC-2020, entry version 68. 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=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., 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. {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; CP000747; ACG78731.1; -; Genomic_DNA. DR RefSeq; WP_012522872.1; NC_011144.1. DR SMR; B4RFG1; -. DR STRING; 450851.PHZ_c2321; -. DR EnsemblBacteria; ACG78731; ACG78731; PHZ_c2321. DR KEGG; pzu:PHZ_c2321; -. DR eggNOG; COG0812; Bacteria. DR HOGENOM; CLU_035304_1_0_5; -. DR OMA; KMNAGMK; -. DR OrthoDB; 841869at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001868; 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; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; -; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; 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; PTHR21071; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR SUPFAM; SSF56194; SSF56194; 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..300 FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase" FT /id="PRO_1000191438" FT DOMAIN 27..216 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 172 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 223 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" FT ACT_SITE 293 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037" 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 //