ID   MURB_AMOA5              Reviewed;         339 AA.
AC   B3ETU4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Aasi_1339;
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2;
RX   PubMed=20023027; DOI=10.1128/jb.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE06646.1; -; Genomic_DNA.
DR   RefSeq; WP_012473390.1; NC_010830.1.
DR   AlphaFoldDB; B3ETU4; -.
DR   SMR; B3ETU4; -.
DR   STRING; 452471.Aasi_1339; -.
DR   EnsemblBacteria; ACE06646; ACE06646; Aasi_1339.
DR   KEGG; aas:Aasi_1339; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_0_0_10; -.
DR   OMA; MQNIGAY; -.
DR   OrthoDB; 841869at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001227; 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..339
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_1000191393"
FT   DOMAIN          16..188
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        238
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00037"
SQ   SEQUENCE   339 AA;  37343 MW;  58815185768C99D0 CRC64;
     MDLQENIPLQ SLNTFGIAAT ARYYSLVKSQ AMLKQLLNNS SLHSLLKLTI GGGSNILFVK
     DFDGWVIHMD IKGIEKLGED NNHIWLHVGA GVNWHSLVLY CIEKGYAGIE NLSLIPGTVG
     AAPIQNIGAY GVEFSEVFES LEALEISTGL IKKFNKEACA FSYRDSIFKS SLKGQYIILQ
     VTLRLNKQPT FQTNYGAIQE VLASMKPRTL SIKAISDAVI YIRQQKLPNP AYIGNAGSFF
     KNPIIDQAKA TLLRNKYPNI PVHILANGYA KLPAAWLIEQ SGWKGYRHDA VGVHLHQPLV
     IVNYGGATGK AVYKLAQAIQ ASVAENFSVM LEPEVNIIQ