MURB_LISMO
ID MURB_LISMO Reviewed; 298 AA.
AC Q8Y776;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=lmo1420;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591979; CAC99498.1; -; Genomic_DNA.
DR PIR; AD1252; AD1252.
DR RefSeq; NP_464945.1; NC_003210.1.
DR RefSeq; WP_010990117.1; NZ_CP023861.1.
DR PDB; 3TX1; X-ray; 2.69 A; A=1-298.
DR PDBsum; 3TX1; -.
DR AlphaFoldDB; Q8Y776; -.
DR SMR; Q8Y776; -.
DR STRING; 169963.lmo1420; -.
DR PaxDb; Q8Y776; -.
DR EnsemblBacteria; CAC99498; CAC99498; CAC99498.
DR GeneID; 984666; -.
DR KEGG; lmo:lmo1420; -.
DR PATRIC; fig|169963.11.peg.1459; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_1_9; -.
DR OMA; MQNIGAY; -.
DR PhylomeDB; Q8Y776; -.
DR BioCyc; LMON169963:LMO1420-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000817; 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 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..298
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179227"
FT DOMAIN 26..191
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3TX1"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3TX1"
FT HELIX 265..283
FT /evidence="ECO:0007829|PDB:3TX1"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:3TX1"
SQ SEQUENCE 298 AA; 32206 MW; 56CB7CDA15613864 CRC64;
MNNLQTKFPH IAIKLNEPLS KYTYTKTGGA ADVFVMPKTI EEAQEVVAYC HQNKIPLTIL
GNGSNLIIKD GGIRGVILHL DLLQTIERNN TQIVAMSGAK LIDTAKFALN ESLSGLEFAC
GIPGSIGGAL HMNAGAYGGE ISDVLEAATV LTQTGELKKL KRSELKAAYR FSTIAEKNYI
VLDATFSLAL EEKNLIQAKM DELTAAREAK QPLEYPSCGS VFKRPPGHFA GKLIQDSGLQ
GHIIGGAQVS LKHAGFIVNI GGATATDYMN LIAYVQQTVR EKFDVELETE VKIIGEDK
