MURB_SYNPW
ID MURB_SYNPW Reviewed; 310 AA.
AC A5GHN8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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};
GN OrderedLocusNames=SynWH7803_0027;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK22453.1; -; Genomic_DNA.
DR RefSeq; WP_011931962.1; NC_009481.1.
DR AlphaFoldDB; A5GHN8; -.
DR SMR; A5GHN8; -.
DR STRING; 32051.SynWH7803_0027; -.
DR EnsemblBacteria; CAK22453; CAK22453; SynWH7803_0027.
DR KEGG; syx:SynWH7803_0027; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_1_3; -.
DR OMA; MQNIGAY; -.
DR OrthoDB; 841869at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001566; 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..310
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000332514"
FT DOMAIN 30..200
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 300
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ SEQUENCE 310 AA; 32752 MW; A8A2DC68ED890788 CRC64;
MSTGTGSLTA LQDCGVLQQK VPLAEFTTWR VGGPAQWLAE PTSTEQIPEL LQWARERRLP
VHMIGAGSNL LIADGGLPGL TLCLRRLQGS ALNADTGRVR AAAGEPLPTL ARRAAKAGLQ
GLEWAVGIPG TVGGAAVMNA GAQGGCTAEQ LISVDVIRFS DAQPSLATLS RDELAFSYRH
SALQSNRHLV VAAEFQLEPG HDPAELQRLT SGNLNHRTST QPYKLPSCGS VFRNPEPEKA
GRLIESLGLK GRAIGGAQVS ELHANFIVNT GDASANDIRA LISLVQGEVM EAKGIALHPE
VKRLGFETPD