MURB_MYCTU
ID MURB_MYCTU Reviewed; 369 AA.
AC P9WJL9; L0T3W0; P65460; Q11148;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; OrderedLocusNames=Rv0482; ORFNames=MTCY20G9.08;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43216.1; -; Genomic_DNA.
DR PIR; E70743; E70743.
DR RefSeq; NP_214996.1; NC_000962.3.
DR RefSeq; WP_003402354.1; NZ_NVQJ01000002.1.
DR PDB; 5JZX; X-ray; 2.20 A; A/B/C/D/E/F=1-369.
DR PDBsum; 5JZX; -.
DR AlphaFoldDB; P9WJL9; -.
DR SMR; P9WJL9; -.
DR STRING; 83332.Rv0482; -.
DR PaxDb; P9WJL9; -.
DR DNASU; 887169; -.
DR GeneID; 45424443; -.
DR GeneID; 887169; -.
DR KEGG; mtu:Rv0482; -.
DR TubercuList; Rv0482; -.
DR eggNOG; COG0812; Bacteria.
DR OMA; MQNIGAY; -.
DR PhylomeDB; P9WJL9; -.
DR BRENDA; 1.3.1.98; 3445.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..369
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179230"
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"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5JZX"
FT TURN 132..138
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5JZX"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5JZX"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5JZX"
FT HELIX 336..354
FT /evidence="ECO:0007829|PDB:5JZX"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5JZX"
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
