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MURB_BUCBP
ID   MURB_BUCBP              Reviewed;         334 AA.
AC   P59450;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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}; OrderedLocusNames=bbp_046;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}.
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         Evidence={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; AE016826; AAO26785.1; -; Genomic_DNA.
DR   RefSeq; WP_011091186.1; NC_004545.1.
DR   AlphaFoldDB; P59450; -.
DR   SMR; P59450; -.
DR   STRING; 224915.bbp_046; -.
DR   EnsemblBacteria; AAO26785; AAO26785; bbp_046.
DR   GeneID; 56470590; -.
DR   KEGG; bab:bbp_046; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_0_0_6; -.
DR   OMA; MQNIGAY; -.
DR   OrthoDB; 841869at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000601; 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..334
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179189"
FT   DOMAIN          16..186
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   334 AA;  38428 MW;  C0703B4E5BA64B05 CRC64;
     MKTYYTSLKK FHTFKINVFA KKIIIVKTIK TLIKTWKKCN QENLPFLLLG KGSNVLFTKN
     YNGFVVVNRI SGITIHEQKD YWLLHVKGGT KWNNLVKYTI QKKIYGLENL ALIPGTVGAA
     PIQNIGAYGV EFKDVCQYVD VLYLNNSKIV RINSNNCLFG YRDSIFKKKH NPNSIILSVG
     IKLPKTWKPK ISHLELQKLS FKNITSHQIF HYICKLRKKK LPNPKKIGNA GSFFKNPIIK
     KNKAHKIICE YKDLPFYPEP HGMIKLSAGW LIEKCKLKNF SVGNAKIYHK QALILINKNN
     LATSKNIIKL AKIIISKVKK KFDITLELEV QIIN
 
 
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