ID   MURB2_BACCR             Reviewed;         305 AA.
AC   Q815R9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase 2;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase 2;
GN   Name=murB2; OrderedLocusNames=BC_5063;
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; AAP11932.1; -; Genomic_DNA.
DR   RefSeq; NP_834731.1; NC_004722.1.
DR   RefSeq; WP_001057102.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q815R9; -.
DR   SMR; Q815R9; -.
DR   STRING; 226900.BC_5063; -.
DR   EnsemblBacteria; AAP11932; AAP11932; BC_5063.
DR   GeneID; 67509724; -.
DR   KEGG; bce:BC5063; -.
DR   PATRIC; fig|226900.8.peg.5222; -.
DR   HOGENOM; CLU_035304_1_1_9; -.
DR   OMA; MQNIGAY; -.
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..305
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase 2"
FT                   /id="PRO_0000179175"
FT   DOMAIN          33..197
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33506 MW;  E269417D2EE5A1ED CRC64;
     MNMQEVYKYL STVLPEGHVK QDEMLKNHTH IKVGGKADVF VAPTNYDEIQ EVIKYANEYN
     IPVTFLGNGS NVIIKDGGIR GITVSLIHIT GVTVTGTTIV AQCGAAIIDV SRIALDHNLT
     GLEFACGIPG SVGGALYMNA GAYGGEISFV LTEAVVMTGD GELRTLTKEA FEFGYRKSVF
     ANNHYIILEA RFELEEGVHE EIKAKMDDLT FKRESKQPLE YPSCGSVFKR PPNNFAGKLI
     QDSGLQGKRI GGVEVSLKHA GFMVNVDNGT AQDYIDLIHF VQKTVEEKFG VKLEREVRII
     GEDKE