ID A0A7W7D1Z2_9ACTN Unreviewed; 378 AA. AC A0A7W7D1Z2; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-MAY-2023, entry version 6. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|HAMAP-Rule:MF_00037}; DE EC=1.3.1.98 {ECO:0000256|HAMAP-Rule:MF_00037}; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00037}; GN Name=murB {ECO:0000256|HAMAP-Rule:MF_00037}; GN ORFNames=BJ982_000378 {ECO:0000313|EMBL:MBB4698834.1}; OS Sphaerisporangium siamense. OC Bacteria; Actinomycetota; Streptosporangiales; Streptosporangiaceae; OC Sphaerisporangium. OX NCBI_TaxID=795645 {ECO:0000313|EMBL:MBB4698834.1, ECO:0000313|Proteomes:UP000542210}; RN [1] {ECO:0000313|EMBL:MBB4698834.1, ECO:0000313|Proteomes:UP000542210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45784 {ECO:0000313|EMBL:MBB4698834.1, RC ECO:0000313|Proteomes:UP000542210}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation. {ECO:0000256|ARBA:ARBA00003921, CC ECO:0000256|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:0000256|ARBA:ARBA00001501, ECO:0000256|HAMAP- CC Rule:MF_00037}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|HAMAP-Rule:MF_00037}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00037}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00037}. CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|ARBA:ARBA00010485, CC ECO:0000256|HAMAP-Rule:MF_00037}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBB4698834.1}. 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; JACHND010000001; MBB4698834.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W7D1Z2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000542210; Unassembled WGS sequence. 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; 3.30.465.10; -; 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 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; 2. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00037}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00037}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00037}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00037}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00037}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00037}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_00037}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00037}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00037}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00037}. FT DOMAIN 17..188 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" FT ACT_SITE 165 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" FT ACT_SITE 243 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" FT ACT_SITE 370 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" SQ SEQUENCE 378 AA; 39500 MW; 6F785BC4A33DB4FF CRC64; MADRVAGVRL APYTTLRVGG PARAFVEAHS GDELVALVAE ADRAGEPVLL LGGGSNLVIS DDGFDGLVVR VATRGVEVHE RDGRAVVTAQ AGEDWDALAA RAVAEGWSGV ECLSGIPGSV GSTPIQNVGA YGQEVAQTIS GVRVYDRRSG TLLDLDAGQC GFAYRHSAFK DDLSRYVVLS VTYELDRTDK SGPVEYKELA ARLGVAIGDR VSLHEARTAV LDLRRGKGMV LDAADPDTCS AGSFFTNPIL DAERAAELKL RAPDFPGWPM PAGAVKVPAA WLIEHAGFPK GYRRGPARIS TKHTLALTNP GGLHVTGFPT DPEAMAVAPS AAGHVAEPSH GAATAADLLA LAREVRDGVE AKFGVTLVNE PILVGLTL //