ID A0A1W1YMK3_9FIRM Unreviewed; 316 AA. AC A0A1W1YMK3; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 14-DEC-2022, entry version 22. 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=SAMN02745168_0543 {ECO:0000313|EMBL:SMC37435.1}; OS Papillibacter cinnamivorans DSM 12816. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae; OC Papillibacter. OX NCBI_TaxID=1122930 {ECO:0000313|EMBL:SMC37435.1, ECO:0000313|Proteomes:UP000192790}; RN [1] {ECO:0000313|EMBL:SMC37435.1, ECO:0000313|Proteomes:UP000192790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12816 {ECO:0000313|EMBL:SMC37435.1, RC ECO:0000313|Proteomes:UP000192790}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) 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|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; FWXW01000001; SMC37435.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1W1YMK3; -. DR STRING; 1122930.SAMN02745168_0543; -. DR EnsemblBacteria; SMC37435; SMC37435; SAMN02745168_0543. DR UniPathway; UPA00219; -. DR Proteomes; UP000192790; 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; 3.30.43.10; -; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000192790}. FT DOMAIN 33..200 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" FT ACT_SITE 179 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" FT ACT_SITE 229 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" FT ACT_SITE 299 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00037" SQ SEQUENCE 316 AA; 33387 MW; 9E81FE150FBAC858 CRC64; MDWVAALAEK LKTRAPGIPL EENVLMSRMT SFRIGGPARL VALPRSGEEL SEAFRCAREM DIDPLPVGNG TNLLVPDRGL DAFVIRTFDG VGDIRCTGEA EISAGAGVLL SRLASFARDC GLAGLEFAHG IPGTLGGAVV MNAGAYGGEM KDAVYEVRAL SETGELMTLR EGELDFSYRH SVFSGGGGVV LGAVLRLAPG DTEGIRGKME ELSARRRQSQ PLEYPSAGSA FKRPPGHFAA ALIQEAGLKG TAVGGAQVSE KHAGFIINRG GATCEDVLRL MDLVRETVFR RSGVTLEPEI KILDGTDLDH PPAAGR //