ID   MURB_LISW6              Reviewed;         297 AA.
AC   A0AIM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   16-MAY-2012, entry version 45.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.1.1.158;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=lwe1437;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 /
OS   SLCC5334).
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / SLCC5334;
RX   PubMed=16936040; DOI=10.1128/JB.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R.,
RA   Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T.,
RA   Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J.,
RA   Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W.,
RA   Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK20855.1; -; Genomic_DNA.
DR   RefSeq; YP_849634.1; NC_008555.1.
DR   ProteinModelPortal; A0AIM3; -.
DR   SMR; A0AIM3; 4-296.
DR   STRING; A0AIM3; -.
DR   GeneID; 4465359; -.
DR   GenomeReviews; AM263198_GR; lwe1437.
DR   KEGG; lwe:lwe1437; -.
DR   PATRIC; 20330017; VBILisWel39304_1443.
DR   eggNOG; COG0812; -.
DR   HOGENOM; HOG000284355; -.
DR   KO; K00075; -.
DR   OMA; SKKHAGF; -.
DR   ProtClustDB; PRK13905; -.
DR   BioCyc; LWEL386043:LWE1437-MONOMER; -.
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   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   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   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    297       UDP-N-acetylenolpyruvoylglucosamine
FT                                reductase.
FT                                /FTId=PRO_1000002894.
FT   DOMAIN       27    191       FAD-binding PCMH-type.
FT   ACT_SITE    170    170       By similarity.
FT   ACT_SITE    220    220       Proton donor (By similarity).
FT   ACT_SITE    290    290       By similarity.
SQ   SEQUENCE   297 AA;  32288 MW;  8A80CFE26F847D53 CRC64;
     MNNLQKQFPH ISIKLNEPLS KYTYTKTGGN ADIFVMPKSI EETQEIVSYC YQNTIPLTVL
     GNGSNLIIKD GGIRGVIVHL DLLQTIERKN TQIIAMSGAK LIDTAKFALG ESLSGLEFAC
     GIPGSIGGAL HMNAGAYGGE ISDVLEAATV LTPYGELKKL KRSELKAAYR FSTIAEKNYI
     VLDATFSLEL EDKNIIQAKM DELTAARESK QPLEYPSCGS VFKRPPGHFA GKLIQDSGLQ
     GHIIGGAQVS LKHAGFIVNI GNATATDYMN LIAHVQQTVR EKFDVELETE VKIIGED
//