ID   MURB1_BACCR             Reviewed;         301 AA.
AC   Q819Q4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase 1;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase 1;
GN   Name=murB1; OrderedLocusNames=BC_3909;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; Evidence={ECO:0000250};
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; AE016877; AAP10830.1; -; Genomic_DNA.
DR   RefSeq; NP_833629.1; NC_004722.1.
DR   RefSeq; WP_000437020.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q819Q4; -.
DR   SMR; Q819Q4; -.
DR   STRING; 226900.BC_3909; -.
DR   EnsemblBacteria; AAP10830; AAP10830; BC_3909.
DR   KEGG; bce:BC3909; -.
DR   PATRIC; fig|226900.8.peg.4031; -.
DR   HOGENOM; CLU_035304_1_1_9; -.
DR   OMA; KMNAGMK; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; 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; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..301
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase 1"
FT                   /id="PRO_0000179174"
FT   DOMAIN          29..196
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32984 MW;  BD1C9BB7F9E331BD CRC64;
     MEQLVNELIE ADVGRVLVNE PLARYTTMKI GGPADILIVP KHVAGIEKTL QLVKQYKTKW
     TVIGRGSNLL VSDQGIEGVV IRLGEGLDHL EVEKHKVRVG SGYPLIKLST LLSRQGLAGL
     EFASGIPGSV GGAVYMNAGA HKSDISSVLS KALILFEDGA IDWLTNKELE FSYRASVLQT
     KRPGIVLEAV FQLQAGKREE IVRSMQNNKD YRRETQPWNH PCAGSVFRNP IPHFAGDLVE
     KAGLRGYRIG GAQISEMHGN FIVNTGGASA QDVLSLIELI KHTIKDKFDV DMHTEVEIIG
     R