MURB_LACLA
ID MURB_LACLA Reviewed; 299 AA.
AC Q9CGD5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; OrderedLocusNames=LL1162; ORFNames=L173881;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}.
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DR EMBL; AE005176; AAK05260.1; -; Genomic_DNA.
DR PIR; B86770; B86770.
DR RefSeq; NP_267318.1; NC_002662.1.
DR RefSeq; WP_010905790.1; NC_002662.1.
DR AlphaFoldDB; Q9CGD5; -.
DR SMR; Q9CGD5; -.
DR STRING; 272623.L173881; -.
DR PaxDb; Q9CGD5; -.
DR EnsemblBacteria; AAK05260; AAK05260; L173881.
DR KEGG; lla:L173881; -.
DR PATRIC; fig|272623.7.peg.1242; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_1_9; -.
DR OMA; MQNIGAY; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002196; 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..299
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179220"
FT DOMAIN 28..193
FT /note="FAD-binding PCMH-type"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 292
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 32098 MW; 8CE430FD281DB4FA CRC64;
MIKETDLENI PDLLVKFNEP LSKYTYTKVG GPADILAFPA TIEALTELLV KAKSTDTAVT
VLGNASNLIV RDGGIRGLVI LLEKLESVKV AGYTIEAQAG AKLKEVTQVA QANSLTGFEF
ACGIPGSIGG AVFMNAGAYG GEISQVLVSC KVMDTDGNIS VLTASEMQFG YRHSVIRDKN
LVVLSAKFEL QAGDPTQIQN EMNRLNFLRE SKQPLEYPSC GSVFKRPVGH FAGQLIQEAN
LQGVRIGGVE VSKKHAGFMV NVANGNATDY EKLIAHVIDK VKENSGVTLE PEVRIIGEK