ID   MURB_BACP2              Reviewed;         303 AA.
AC   A8FCY2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   12-SEP-2018, entry version 76.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000255|HAMAP-Rule:MF_00037};
DE            EC=1.3.1.98 {ECO:0000255|HAMAP-Rule:MF_00037};
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00037};
GN   Name=murB {ECO:0000255|HAMAP-Rule:MF_00037};
GN   OrderedLocusNames=BPUM_1416;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA   Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA   Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA   Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA   Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA   Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA   Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-
CC       N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.
CC       {ECO:0000255|HAMAP-Rule:MF_00037}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00037};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00037}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00037}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00037}.
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DR   EMBL; CP000813; ABV62099.1; -; Genomic_DNA.
DR   RefSeq; WP_012009870.1; NC_009848.4.
DR   ProteinModelPortal; A8FCY2; -.
DR   SMR; A8FCY2; -.
DR   STRING; 315750.BPUM_1416; -.
DR   PRIDE; A8FCY2; -.
DR   EnsemblBacteria; ABV62099; ABV62099; BPUM_1416.
DR   KEGG; bpu:BPUM_1416; -.
DR   eggNOG; ENOG4105D4A; Bacteria.
DR   eggNOG; COG0812; LUCA.
DR   HOGENOM; HOG000284355; -.
DR   KO; K00075; -.
DR   OMA; KMNAGMK; -.
DR   OrthoDB; POG091H0270; -.
DR   BioCyc; BPUM315750:G1G9U-1469-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001355; 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:InterPro.
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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.90.78.10; -; 1.
DR   HAMAP; MF_00037; MurB; 1.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR036318; FAD-bd_2-like_sf.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
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;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD;
KW   Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN         1    303       UDP-N-acetylenolpyruvoylglucosamine
FT                                reductase.
FT                                /FTId=PRO_1000057272.
FT   DOMAIN       30    196       FAD-binding PCMH-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    174    174       {ECO:0000255|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    225    225       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00037}.
FT   ACT_SITE    295    295       {ECO:0000255|HAMAP-Rule:MF_00037}.
SQ   SEQUENCE   303 AA;  33353 MW;  DF29FD0990A96454 CRC64;
     MENLKNELLE AQVGKVLENE PLANHTTMKI GGPADLLIIP KDIDAVKTIM DHVKKHQTNW
     TVIGRGSNLL VLDKGIRGVV LKLGTGLDHL TVNDEEITVG GGYSVVRLAT SLSKQGLSGL
     EFAAGIPGSI GGAVYMNAGA HGSDISKILV KARILFEDGS IEWLTNEQMN FSYRTSVLQK
     ERPGIVLEAV FKLKQDDREK ITKKMQQNKD YRKETQPYNR PCAGSIFRNP LPEYAGQLVE
     KANLKGYQLG GARISDMHGN FIVNAGGATA QDVLDLIQFI QKKIKEDYNV EMHTEVEIIG
     EEN
//