ID   MURB_RICPR              Reviewed;         295 AA.
AC   Q9ZDS7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=RP248;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA14710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ235271; CAA14710.1; ALT_INIT; Genomic_DNA.
DR   PIR; D71679; D71679.
DR   RefSeq; NP_220633.1; NC_000963.1.
DR   RefSeq; WP_004598530.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDS7; -.
DR   SMR; Q9ZDS7; -.
DR   STRING; 272947.RP248; -.
DR   EnsemblBacteria; CAA14710; CAA14710; CAA14710.
DR   GeneID; 57569376; -.
DR   KEGG; rpr:RP248; -.
DR   PATRIC; fig|272947.5.peg.255; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_0_5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002480; Chromosome.
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:UniProtKB-UniRule.
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-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..295
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179251"
FT   DOMAIN          24..188
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  32752 MW;  D59581825E9F0BAC CRC64;
     MSILPIIKGE YKKDYNLKHL TWFKVGGNAE IFFKPFDFAD LKSFLIQNKQ KLPITTFGSG
     SNIIIRDGGI EGVVIKLGQN FNKIEFLDNH LIVGSSCLNY NLARFCQANA ISGFEFLVGI
     PGTIGGGVIM NAGAYGSAFQ DIIVQVEALD FSGNFLTFTN KEIGFKYRGN NLPKDLILLK
     AVFKVNKGDS QNILLKMNKI NNTRSSTQPI KERTGGSTFI NPEGRKSWEL IDKAGLRGYR
     IGGASISELH CNFMINNGNA TAKDLEDLGN FVRQKVFEDS GVELNWEIKR IGKYV