ID   MURB_AQUAE              Reviewed;         297 AA.
AC   O66805;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=aq_520;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(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}.
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DR   EMBL; AE000657; AAC06766.1; -; Genomic_DNA.
DR   PIR; A70347; A70347.
DR   RefSeq; NP_213365.1; NC_000918.1.
DR   RefSeq; WP_010880303.1; NC_000918.1.
DR   AlphaFoldDB; O66805; -.
DR   SMR; O66805; -.
DR   STRING; 224324.aq_520; -.
DR   EnsemblBacteria; AAC06766; AAC06766; aq_520.
DR   KEGG; aae:aq_520; -.
DR   PATRIC; fig|224324.8.peg.427; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_1_0; -.
DR   InParanoid; O66805; -.
DR   OMA; MQNIGAY; -.
DR   OrthoDB; 841869at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000798; 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..297
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179171"
FT   DOMAIN          16..182
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  33266 MW;  0E9BD1FDF938797B CRC64;
     MLFLKNVPLQ NLTTIKIGGR VSFYAEPSDL KEISLCIDFS KSRDIPLFVL GNGSNTIFGD
     VRGLVVNLKN LKGFKVKEIK GKFFVEAFSG TPLKDLIRFS VKENVKSFYK LLGFPASVGG
     AVSMNAGAFG VEISDFLKEV YFVDWEGKLQ KAKRDELNFS YRKSPFPKLG IVFKVVFEFE
     RSKENILPKY EKIRRIRKEK QPINLPTSGS TFKNPEGNFA GKLLEKAGLK GFRLKNVGFS
     EKHANFLVNY GGGTFSEVVD LINIAKERVY ENFGIVLEEE VKLIESSGSD GWKVLGA