MURB_ECOLI
ID MURB_ECOLI Reviewed; 342 AA.
AC P08373; Q2M8R3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; Synonyms=yijB; OrderedLocusNames=b3972, JW3940;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=3899863; DOI=10.1016/0378-1119(85)90011-3;
RA Howard P.K., Shaw J., Otsuka A.J.;
RT "Nucleotide sequence of the birA gene encoding the biotin operon repressor
RT and biotin holoenzyme synthetase functions of Escherichia coli.";
RL Gene 35:321-331(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=1311302; DOI=10.1128/jb.174.5.1690-1693.1992;
RA Pucci M.J., Discotto L.F., Dougherty T.J.;
RT "Cloning and identification of the Escherichia coli murB DNA sequence,
RT which encodes UDP-N-acetylenolpyruvoylglucosamine reductase.";
RL J. Bacteriol. 174:1690-1693(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
RX PubMed=7028991; DOI=10.1016/0022-2836(81)90508-8;
RA Brosius J., Dull T.J., Sleeter D.D., Noller H.F.;
RT "Gene organization and primary structure of a ribosomal RNA operon from
RT Escherichia coli.";
RL J. Mol. Biol. 148:107-127(1981).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8448160; DOI=10.1021/bi00059a019;
RA Benson T.E., Marquardt J.L., Marquardt A.C., Etzkorn F.A., Walsh C.T.;
RT "Overexpression, purification, and mechanistic study of UDP-N-
RT acetylenolpyruvylglucosamine reductase.";
RL Biochemistry 32:2024-2030(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8805513; DOI=10.1016/s0969-2126(96)00008-1;
RA Benson T.E., Walsh C.T., Hogle J.M.;
RT "The structure of the substrate-free form of MurB, an essential enzyme for
RT the synthesis of bacterial cell walls.";
RL Structure 4:47-54(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9020778; DOI=10.1021/bi962221g;
RA Benson T.E., Walsh C.T., Hogle J.M.;
RT "X-ray crystal structures of the S229A mutant and wild-type MurB in the
RT presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A
RT resolution.";
RL Biochemistry 36:806-811(1997).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=9150408; DOI=10.1006/jmbi.1997.0915;
RA Constantine K.L., Mueller L., Goldfarb V., Wittekind M., Metzler W.J.,
RA Yanchunas J. Jr., Robertson J.G., Malley M.F., Friedrichs M.S.,
RA Farmer B.T. II;
RT "Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR
RT assignments and chemical-shift changes.";
RL J. Mol. Biol. 267:1223-1246(1997).
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:0000305}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR EMBL; M10123; AAA23519.1; -; Genomic_DNA.
DR EMBL; L14557; AAA24185.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43074.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76950.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77343.1; -; Genomic_DNA.
DR EMBL; V00348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A24029; QQECB8.
DR RefSeq; NP_418403.1; NC_000913.3.
DR RefSeq; WP_001016699.1; NZ_SSZK01000084.1.
DR PDB; 1MBB; X-ray; 2.30 A; A=1-342.
DR PDB; 1MBT; X-ray; 3.00 A; A=1-342.
DR PDB; 1UXY; X-ray; 1.80 A; A=3-342.
DR PDB; 2MBR; X-ray; 1.80 A; A=3-342.
DR PDB; 2Q85; X-ray; 2.51 A; A=1-342.
DR PDBsum; 1MBB; -.
DR PDBsum; 1MBT; -.
DR PDBsum; 1UXY; -.
DR PDBsum; 2MBR; -.
DR PDBsum; 2Q85; -.
DR AlphaFoldDB; P08373; -.
DR SMR; P08373; -.
DR BioGRID; 4262982; 592.
DR BioGRID; 852766; 2.
DR DIP; DIP-10277N; -.
DR IntAct; P08373; 12.
DR STRING; 511145.b3972; -.
DR BindingDB; P08373; -.
DR ChEMBL; CHEMBL5526; -.
DR DrugBank; DB07296; (5Z)-3-(4-CHLOROPHENYL)-4-HYDROXY-5-(1-NAPHTHYLMETHYLENE)FURAN-2(5H)-ONE.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR jPOST; P08373; -.
DR PaxDb; P08373; -.
DR PRIDE; P08373; -.
DR EnsemblBacteria; AAC76950; AAC76950; b3972.
DR EnsemblBacteria; BAE77343; BAE77343; BAE77343.
DR GeneID; 948470; -.
DR KEGG; ecj:JW3940; -.
DR KEGG; eco:b3972; -.
DR PATRIC; fig|1411691.4.peg.2736; -.
DR EchoBASE; EB1190; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_0_0_6; -.
DR InParanoid; P08373; -.
DR OMA; MQNIGAY; -.
DR PhylomeDB; P08373; -.
DR BioCyc; EcoCyc:UDPNACETYLMURAMATEDEHYDROG-MON; -.
DR BioCyc; MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MON; -.
DR SABIO-RK; P08373; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P08373; -.
DR PRO; PR:P08373; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoliWiki.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IDA:EcoCyc.
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; IMP:EcoliWiki.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..342
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179207"
FT DOMAIN 13..183
FT /note="FAD-binding PCMH-type"
FT ACT_SITE 159
FT ACT_SITE 229
FT /note="Proton donor"
FT ACT_SITE 325
FT BINDING 190
FT /ligand="substrate"
FT CONFLICT 35
FT /note="Y -> H (in Ref. 2; AAA24185)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> C (in Ref. 2; AAA24185)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="K -> E (in Ref. 2; AAA24185)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="I -> M (in Ref. 2; AAA24185)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1UXY"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1UXY"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1UXY"
FT TURN 165..170
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:1UXY"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:1UXY"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2Q85"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1UXY"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1UXY"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2MBR"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:1UXY"
SQ SEQUENCE 342 AA; 37851 MW; F43CFE29251E45C6 CRC64;
MNHSLKPWNT FGIDHNAQHI VCAEDEQQLL NAWQYATAEG QPVLILGEGS NVLFLEDYRG
TVIINRIKGI EIHDEPDAWY LHVGAGENWH RLVKYTLQEG MPGLENLALI PGCVGSSPIQ
NIGAYGVELQ RVCAYVDSVE LATGKQVRLT AKECRFGYRD SIFKHEYQDR FAIVAVGLRL
PKEWQPVLTY GDLTRLDPTT VTPQQVFNAV CHMRTTKLPD PKVNGNAGSF FKNPVVSAET
AKALLSQFPT APNYPQADGS VKLAAGWLID QCQLKGMQIG GAAVHRQQAL VLINEDNAKS
EDVVQLAHHV RQKVGEKFNV WLEPEVRFIG ASGEVSAVET IS
