ID A0A496JZF8_STRSP Unreviewed; 191 AA. AC A0A496JZF8; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 18-SEP-2019, entry version 4. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000256|SAAS:SAAS00232078}; DE EC=1.3.1.98 {ECO:0000256|SAAS:SAAS00057125}; DE Flags: Fragment; GN Name=murB {ECO:0000313|EMBL:RKV69641.1}; GN ORFNames=D8H99_63665 {ECO:0000313|EMBL:RKV69641.1}; OS Streptococcus sp. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1306 {ECO:0000313|EMBL:RKV69641.1, ECO:0000313|Proteomes:UP000276398}; RN [1] {ECO:0000313|Proteomes:UP000276398} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Espinoza J.L., Harkins D., Torralba M., Gomez A., Highlander S., RA Jones M., Leong P., Saffery R., Bockmann M., Kuelbs C., Inman J., RA Hughes T., Craig J.M., Nelson K.E., Dupont C.; RT "Supragingival plaque microbiome ecology and functional potential in RT the context of health and disease (bins)."; RL bioRxivorg 0:0-0(2018). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|SAAS:SAAS00057166}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + CC UDP-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; CC EC=1.3.1.98; Evidence={ECO:0000256|SAAS:SAAS01115694}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|SAAS:SAAS00170035}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|SAAS:SAAS00057202}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00057122}. CC -!- SIMILARITY: Belongs to the MurB family. CC {ECO:0000256|SAAS:SAAS00558987}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RKV69641.1}. 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; RBKM01003793; RKV69641.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000276398; 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:InterPro. 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-UniPathway. 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; -; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; IPR016166; FAD-bd_PCMH. DR InterPro; IPR036318; FAD-bd_PCMH-like_sf. 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 {ECO:0000256|SAAS:SAAS00445367}; KW Cell division {ECO:0000256|SAAS:SAAS00445259}; KW Cell shape {ECO:0000256|SAAS:SAAS00445137}; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00445388}; KW Complete proteome {ECO:0000313|Proteomes:UP000276398}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00098084}; KW FAD {ECO:0000256|SAAS:SAAS00098222}; KW Flavoprotein {ECO:0000256|SAAS:SAAS00445343}; KW NADP {ECO:0000256|SAAS:SAAS00445332}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00098144, KW ECO:0000313|EMBL:RKV69641.1}; KW Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00445231}. FT DOMAIN 1 84 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. FT NON_TER 1 1 {ECO:0000313|EMBL:RKV69641.1}. SQ SEQUENCE 191 AA; 20665 MW; D9B31D15698BE013 CRC64; ALRHSLTGFE FACGIPGSIG GAVFMNAGAY GGEIAHILQS CQILTKEGEI ETLSVKDLAF GYRHSAIQDS GAIVLSAKFA LAPGNHQVIK QEMDRLTHLR ELKQPLEYPS CGSVFKRPVG HFAGQLISEA GLKGYRIGGV EVSEKHAGFM INVADGTARD YEDLIESVIE KVKEHSGVTL EREVRILGEK E //