ID   MURB_SALTY              Reviewed;         342 AA.
AC   P37417;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=STM4137; ORFNames=STMF1.1;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=8048842; DOI=10.1007/bf00307771;
RA   Dombrosky P.M., Schmid M.B., Young K.D.;
RT   "Sequence divergence of the murB and rrfB genes from Escherichia coli and
RT   Salmonella typhimurium.";
RL   Arch. Microbiol. 161:501-507(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Cell wall formation.
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;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR   EMBL; L14816; AAA27163.1; -; Genomic_DNA.
DR   EMBL; AF170176; AAF33492.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22970.1; -; Genomic_DNA.
DR   RefSeq; NP_463011.1; NC_003197.2.
DR   RefSeq; WP_000149795.1; NC_003197.2.
DR   AlphaFoldDB; P37417; -.
DR   SMR; P37417; -.
DR   STRING; 99287.STM4137; -.
DR   PaxDb; P37417; -.
DR   EnsemblBacteria; AAL22970; AAL22970; STM4137.
DR   GeneID; 1255663; -.
DR   KEGG; stm:STM4137; -.
DR   PATRIC; fig|99287.12.peg.4353; -.
DR   HOGENOM; CLU_035304_0_0_6; -.
DR   OMA; MQNIGAY; -.
DR   PhylomeDB; P37417; -.
DR   BioCyc; SENT99287:STM4137-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; 3.30.43.10; -; 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..342
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179253"
FT   DOMAIN          13..183
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  37647 MW;  B3FBE860EB32BEFA CRC64;
     MTHSLKPWNT FGIDHCAKHI VCAENEQQLL SAWQQATREG LPVMILGEGS NVLFLENYAG
     TVILNRLKGI EVNETADAWH LHVGAGENWH QLVRYALDNN MPGLENLALI PGCVGSSPIQ
     NIGAYGVELQ RVCDYVDCVE LETGKRLRLS AAECRFGYRD SIFKNEYQDR VAIVAVGLRL
     SKQWQPVLTY GDLTCLDPKT VTAQQVFDAV CHMRTTKLPD PKVNGNAGSF FKNPVVAADI
     AMELLERFPN APHYPQADGS VKLAAGWLID QCQLKGVTIG GAAVHRQQAL VLINANDATS
     KDVVALAHHV RQKVGEKFNV WLEPEVRFIG RSGEVNAVES IA