ID   MURB_BORPE              Reviewed;         351 AA.
AC   Q9X6Y8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=BP2510;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RA   Pradel E.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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; AJ238308; CAB41011.1; -; Genomic_DNA.
DR   EMBL; BX640418; CAE42782.1; -; Genomic_DNA.
DR   RefSeq; NP_881137.1; NC_002929.2.
DR   RefSeq; WP_010930965.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q9X6Y8; -.
DR   SMR; Q9X6Y8; -.
DR   STRING; 257313.BP2510; -.
DR   GeneID; 45388866; -.
DR   GeneID; 56477570; -.
DR   KEGG; bpe:BP2510; -.
DR   PATRIC; fig|257313.5.peg.2708; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_0_0_4; -.
DR   OMA; MQNIGAY; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002676; 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..351
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179183"
FT   DOMAIN          29..199
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  37364 MW;  81E10E9A148B70F2 CRC64;
     MSTVPARIEP VAPLAPQAQD LRCFNTLGLA SHAPAFVALT EPSQLPALSA LAPRFRQLVV
     LGGGSNVVLP ASIDGLVAQV RLPGVRLVGQ CADAWVVEAA AGENWHGFVT ACVDNGWDGL
     ENLALIPGTV GAAPVQNIGA YGVELADRFH SLTAWDVKGG RWVEMGAAEC RFAYRDSFFK
     HQEPGAWVIG SVRFALPRPW QPVLDYPDLQ RHAALDGAAP TARAVYDAVC AIRRAKLPDP
     AVVGNAGSFF KNPLVDAGTR QALLGRFPGL VSYPQPDGRY KLAAGWLIDQ CGWKGRQLGA
     AGVHDRQALV LVNRGGAQAR DIMALAAAIQ GDVERRYGVR LEPEPVVVPA R