MURB_BUCAI
ID MURB_BUCAI Reviewed; 356 AA.
AC P57153;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE EC=1.3.1.98;
DE AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN Name=murB; OrderedLocusNames=BU045;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12768.1; -; Genomic_DNA.
DR RefSeq; NP_239882.1; NC_002528.1.
DR RefSeq; WP_010895915.1; NC_002528.1.
DR AlphaFoldDB; P57153; -.
DR SMR; P57153; -.
DR STRING; 107806.10038733; -.
DR EnsemblBacteria; BAB12768; BAB12768; BAB12768.
DR KEGG; buc:BU045; -.
DR PATRIC; fig|107806.10.peg.54; -.
DR eggNOG; COG0812; Bacteria.
DR HOGENOM; CLU_035304_0_0_6; -.
DR OMA; MQNIGAY; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001806; 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..356
FT /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT /id="PRO_0000179187"
FT DOMAIN 20..190
FT /note="FAD-binding PCMH-type"
FT ACT_SITE 166
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 40593 MW; 103486BF1DE25EA7 CRC64;
MHKKKYFSSQ SLKDLNTFAI DVTAKKIIFV KTIQSLIDIS KICQLSNIPY IILGEGSNVL
FLENYVGVVI INRIKGIKIV EKKNFWLLHV FSGEKWHNLV KLTLNLGILG LENLALIPGC
IGSAAIQNIG AYGLEFKDVC QYVDILSLKD NTIKRIYKNS CKFSYRNSIF KDQYKNEHAV
IRVGIKLSKK WRPILFSSLE NYITPINITA YKIFNIICKI RKKKLPDPKK IGNAGSFFKN
PLIKKKKAQK LINLYKVPNY PQKNGLVKIS AAWLIENYKF KHLQIGDAAI HKKQKLILIN
KKNATAQEII KLAKIIHKCI LKKFNILLEP EVDLIGASGK IKASKIFKLN SKLKVI