ID   MURB_TRIL1              Reviewed;         302 AA.
AC   B3E3Y0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Glov_0668;
OS   Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS   lovleyi).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Trichlorobacter.
OX   NCBI_TaxID=398767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA   Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001089; ACD94394.1; -; Genomic_DNA.
DR   RefSeq; WP_012468750.1; NC_010814.1.
DR   AlphaFoldDB; B3E3Y0; -.
DR   SMR; B3E3Y0; -.
DR   STRING; 398767.Glov_0668; -.
DR   EnsemblBacteria; ACD94394; ACD94394; Glov_0668.
DR   KEGG; glo:Glov_0668; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_1_7; -.
DR   OMA; KMNAGMK; -.
DR   OrthoDB; 841869at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002420; 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..302
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_1000191423"
FT   DOMAIN          29..192
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   302 AA;  32804 MW;  215BDA0E39AF1CD9 CRC64;
     MHAGLEHIRD WFKGELLFHE PLARHVSLKV GGPVDLLATP DSREELQQLV TLLDQQQIPR
     FVLGGGFNLL PSDVGYRGCA ISLKQINRLQ LDDTVVAIEA GASNQSLARA VAELGLSGIE
     FLIGIPGSVG GAVRMNAGAH GSDIFSVVKT VTLLDQGQFR ELPREQLTYG YRCFEIPDNS
     VIVAVTLQLS EDSLQAVRSR MEEQLGLRWA TQNVKFPNAG SFFKNPPGES AWRLIDQAGL
     RGFSIGNAQV SEVHTNFLIN RGNATAADFR ALAAAVKERV KATCGIELEE EVQLLDSGEC
     GQ