ID MURB_MYCTO Reviewed; 369 AA.
AC P9WJL8; L0T3W0; P65460; Q11148;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; OrderedLocusNames=MT0500;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44723.1; -; Genomic_DNA.
DR PIR; E70743; E70743.
DR RefSeq; WP_003402354.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJL8; -.
DR SMR; P9WJL8; -.
DR GeneID; 45424443; -.
DR KEGG; mtc:MT0500; -.
DR PATRIC; fig|83331.31.peg.530; -.
DR HOGENOM; CLU_035304_0_1_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001020; 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; 3.30.465.10; -; 1.
DR Gene3D; 3.90.78.10; UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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 NCBIfam; TIGR00179; murB; 1.
DR PANTHER; PTHR21071; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR PANTHER; PTHR21071:SF4; UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF02873; MurB_C; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56194; Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain; 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..369
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000427807"
FT DOMAIN 29..202
FT /note="FAD-binding PCMH-type"
FT ACT_SITE 176
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 38521 MW; 50AC021602ED9822 CRC64;
MKRSGVGSLF AGAHIAEAVP LAPLTTLRVG PIARRVITCT SAEQVVAALR HLDSAAKTGA
DRPLVFAGGS NLVIAENLTD LTVVRLANSG ITIDGNLVRA EAGAVFDDVV VRAIEQGLGG
LECLSGIPGS AGATPVQNVG AYGAEVSDTI TRVRLLDRCT GEVRWVSARD LRFGYRTSVL
KHADGLAVPT VVLEVEFALD PSGRSAPLRY GELIAALNAT SGERADPQAV REAVLALRAR
KGMVLDPTDH DTWSVGSFFT NPVVTQDVYE RLAGDAATRK DGPVPHYPAP DGVKLAAGWL
VERAGFGKGY PDAGAAPCRL STKHALALTN RGGATAEDVV TLARAVRDGV HDVFGITLKP
EPVLIGCML
//
