ID   MURB_BACLI              Reviewed;         184 AA.
AC   Q45305;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
DE   Flags: Fragment;
GN   Name=murB;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5A2;
RX   PubMed=8088553; DOI=10.1016/0378-1119(94)90043-4;
RA   Harry E.J., Partridge S.R., Weiss A.S., Wake R.G.;
RT   "Conservation of the 168 divIB gene in Bacillus subtilis W23 and B.
RT   licheniformis, and evidence for homology to ftsQ of Escherichia coli.";
RL   Gene 147:85-89(1994).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR   EMBL; U01958; AAA57244.1; -; Genomic_DNA.
DR   PIR; I40220; I40220.
DR   AlphaFoldDB; Q45305; -.
DR   SMR; Q45305; -.
DR   UniPathway; UPA00219; -.
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:UniProtKB-EC.
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; 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   PANTHER; PTHR21071; PTHR21071; 1.
DR   Pfam; PF02873; MurB_C; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   SUPFAM; SSF56194; SSF56194; 1.
DR   TIGRFAMs; TIGR00179; murB; 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.
FT   CHAIN           <1..184
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179177"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   184 AA;  20166 MW;  4114D8B29AE21EFD CRC64;
     LEFAAGIPGS VGGAVYMNAG AHGSDISRVL VKALILFEDG TIDWLTNEEM AFSYRTSILQ
     NERPGICLEA VLQLEQKERD EIVAQMQKNK DYRKETQPVS NPCAGSIFRN PLPEHAGRLV
     DEAGLKGHQI GGAKVSEMHG NFIVNAGGAT AQDVLDLIAF IQKTIKEKYD IDMHTEVEII
     GEKR