MURB_RUEST
ID MURB_RUEST Reviewed; 308 AA.
AC Q1GIU8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=TM1040_0685;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
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; CP000377; ABF63418.1; -; Genomic_DNA.
DR RefSeq; WP_011538030.1; NC_008044.1.
DR AlphaFoldDB; Q1GIU8; -.
DR SMR; Q1GIU8; -.
DR STRING; 292414.TM1040_0685; -.
DR EnsemblBacteria; ABF63418; ABF63418; TM1040_0685.
DR KEGG; sit:TM1040_0685; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_1_0_5; -.
DR OMA; KMNAGMK; -.
DR OrthoDB; 841869at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000636; 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..308
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_1000002912"
FT DOMAIN 24..187
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT REGION 198..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 298
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ SEQUENCE 308 AA; 32917 MW; F58293D0F6CFCF8F CRC64;
MTDLPAVRGR LTPNRDLSDL TWLRVGGPAD YLFQPADLED LQEFLRNLPA DMDVFPMGVG
SNLIVRDGGL RSVVIRLGRG FNGIEVDGDT VTAGAAALDA HVARKSAEAG VDLTFLRTIP
GSIGGAVRMN AGCYGSYVAD VFMSAQVVLR DGSLATLSAE DLQFKYRQTE LAPGAVLVSA
TLRGPKGDPD ALAARMEDQL RKRDETQPTK ERSAGSTFRN PAGFSSTGKA DDVMDLKAWK
VIDNAGLRGA TLGGAQMSEK HSNFMINAGG ATAADLEGLG ENVRKKVYAD SGIWLEWEIM
RVGDPKRS
