MURB_STAAU
ID MURB_STAAU Reviewed; 307 AA.
AC P61431; Q93G02;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.3
RP ANGSTROMS).
RC STRAIN=ISP3;
RX PubMed=11327854; DOI=10.1021/bi002162d;
RA Benson T.E., Harris M.S., Choi G.H., Cialdella J.I., Herberg J.T.,
RA Martin J.P. Jr., Baldwin E.T.;
RT "A structural variation for MurB: X-ray crystal structure of Staphylococcus
RT aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB).";
RL Biochemistry 40:2340-2350(2001).
CC -!- FUNCTION: Cell wall formation.
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 -!- 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; AF300988; AAK97215.1; -; Genomic_DNA.
DR RefSeq; WP_000608440.1; NZ_WTUM01000027.1.
DR PDB; 1HSK; X-ray; 2.30 A; A=2-307.
DR PDBsum; 1HSK; -.
DR AlphaFoldDB; P61431; -.
DR SMR; P61431; -.
DR BindingDB; P61431; -.
DR ChEMBL; CHEMBL4089; -.
DR OMA; MQNIGAY; -.
DR BioCyc; MetaCyc:MON-12254; -.
DR BRENDA; 1.3.1.98; 3352.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P61431; -.
DR PRO; PR:P61431; -.
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.
FT CHAIN 1..307
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179261"
FT DOMAIN 33..197
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT ACT_SITE 176
FT ACT_SITE 226
FT /note="Proton donor"
FT ACT_SITE 296
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1HSK"
FT TURN 168..172
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1HSK"
FT HELIX 271..289
FT /evidence="ECO:0007829|PDB:1HSK"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1HSK"
SQ SEQUENCE 307 AA; 33797 MW; 8F5C3E89F7EAE0A0 CRC64;
MINKDIYQAL QQLIPNEKIK VDEPLKRYTY TKTGGNADFY ITPTKNEEVQ AVVKYAYQNE
IPVTYLGNGS NIIIREGGIR GIVISLLSLD HIEVSDDAII AGSGAAIIDV SRVARDYALT
GLEFACGIPG SIGGAVYMNA GAYGGEVKDC IDYALCVNEQ GSLIKLTTKE LELDYRNSII
QKEHLVVLEA AFTLAPGKMT EIQAKMDDLT ERRESKQPLE YPSCGSVFQR PPGHFAGKLI
QDSNLQGHRI GGVEVSTKHA GFMVNVDNGT ATDYENLIHY VQKTVKEKFG IELNREVRII
GEHPKES
