MURB_BACLD
ID MURB_BACLD Reviewed; 303 AA.
AC Q65JX9; Q62VD0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=BLi01740, BL02244;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU40635.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23278.1; -; Genomic_DNA.
DR RefSeq; WP_003181550.1; NC_006322.1.
DR PDB; 4PYT; X-ray; 1.85 A; A=1-303.
DR PDBsum; 4PYT; -.
DR AlphaFoldDB; Q65JX9; -.
DR SMR; Q65JX9; -.
DR STRING; 279010.BL02244; -.
DR PRIDE; Q65JX9; -.
DR EnsemblBacteria; AAU23278; AAU23278; BL02244.
DR GeneID; 66216247; -.
DR KEGG; bld:BLi01740; -.
DR KEGG; bli:BL02244; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_1_9; -.
DR OMA; KMNAGMK; -.
DR OrthoDB; 841869at2; -.
DR BioCyc; BLIC279010:BLI_RS08605-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000606; 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 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..303
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000224659"
FT DOMAIN 29..196
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 225
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 295
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4PYT"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4PYT"
FT HELIX 270..288
FT /evidence="ECO:0007829|PDB:4PYT"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:4PYT"
SQ SEQUENCE 303 AA; 32810 MW; FBE18626B21B07A7 CRC64;
MDKVIQELKE LEVGKVLENE PLSNHTTIKI GGPADVLVIP KDIQAVKDTM KVVKKHGVKW
TAIGRGSNLL VLDEGIRGVV IKLGQGLDHM EIDGEQVTVG GGYSVVRLAT GISKKGLSGL
EFAAGIPGSV GGAVYMNAGA HGSDISKVLV KALILFEDGT IEWLTNEEMA FSYRTSILQN
KRPGICLEAV LQLEQKERDQ IVAQMQKNKD YRKETQPVSN PCAGSIFRNP LPEHAGRLVE
EAGLKGHQIG GAKVSEMHGN FIVNAGGATA KDVLDLIAFI QKTIKEKYDI DMHTEVEIIG
EKR
