ID   MURB_HELPY              Reviewed;         259 AA.
AC   O25963;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=HP_1418;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD08460.1; -; Genomic_DNA.
DR   PIR; B64697; B64697.
DR   RefSeq; NP_208209.1; NC_000915.1.
DR   RefSeq; WP_000894903.1; NC_018939.1.
DR   AlphaFoldDB; O25963; -.
DR   SMR; O25963; -.
DR   STRING; 85962.C694_07335; -.
DR   PaxDb; O25963; -.
DR   EnsemblBacteria; AAD08460; AAD08460; HP_1418.
DR   KEGG; hpy:HP_1418; -.
DR   PATRIC; fig|85962.47.peg.1522; -.
DR   eggNOG; COG0812; Bacteria.
DR   OMA; KMNAGMK; -.
DR   PhylomeDB; O25963; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 3.30.465.10; -; 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; Reference proteome.
FT   CHAIN           1..259
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179218"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   259 AA;  28592 MW;  9C0B4621DF39F01D CRC64;
     MLETTIDFSR YSSVKIGTPL KVSVLENDDE ISQEHQIIGL ANNLLIAPSA KNLALLGKNY
     DYICDKGECV EIGGAANASK IFNYFRANDL EGLEFLGQLP GTLGALVKMN AGMKEFEIKN
     VLESACINNQ WLEKEALGLG YRSSGFSGVV LRARFKKTHG FREGVLKACQ SMRKSHPKLP
     NFGSCFKNPP NDHAGRLLEG VGLRGYCLKR VGFAKEHANF LVNLGGAEFE EALDLIELAK
     ARVLQEYGIH LEEEVKILR