(data stored in ACNUC29543 zone)

SWISSPROT: MURB_SYNR3

ID   MURB_SYNR3              Reviewed;         305 AA.
AC   A5GPX0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
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};
GN   OrderedLocusNames=SynRCC307_0026;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 +
CC         UDP-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;
CC         EC=1.3.1.98; 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}.
DR   EMBL; CT978603; CAK26929.1; -; Genomic_DNA.
DR   RefSeq; WP_011934444.1; NC_009482.1.
DR   SMR; A5GPX0; -.
DR   STRING; 316278.SynRCC307_0026; -.
DR   PRIDE; A5GPX0; -.
DR   EnsemblBacteria; CAK26929; CAK26929; SynRCC307_0026.
DR   KEGG; syr:SynRCC307_0026; -.
DR   eggNOG; ENOG4105D4A; Bacteria.
DR   eggNOG; COG0812; LUCA.
DR   HOGENOM; HOG000284355; -.
DR   KO; K00075; -.
DR   OMA; IGNAGSF; -.
DR   OrthoDB; 841869at2; -.
DR   BioCyc; SSP316278:G1GJL-26-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001115; 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;
DR   PRODOM; A5GPX0.
DR   SWISS-2DPAGE; A5GPX0.
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD;
KW   Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN         1    305       UDP-N-acetylenolpyruvoylglucosamine
FT                                reductase.
FT                                /FTId=PRO_0000332513.
FT   DOMAIN       22    190       FAD-binding PCMH-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    169    169       {ECO:0000255|HAMAP-Rule:MF_00037}.
FT   ACT_SITE    220    220       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00037}.
FT   ACT_SITE    290    290       {ECO:0000255|HAMAP-Rule:MF_00037}.
SQ   SEQUENCE   305 AA;  32203 MW;  D5DE9BC682F67836 CRC64;
     MEIPADLNLR KDVPLGDFTT WKVGGAADFF AEPDSSDHLE ALVHWGRGQQ LPMRFIGAGS
     NLLISDEGLA GLVICSRRLQ GSQLDPTTGI IEAQAGEPLP TLARRAAKAG LSGLEWSVGI
     PGTVGGAVVM NAGAQGGCIA ESLIDATVLD PSSGQTRRMS CNELDYDYRH SALQSEALVV
     LSARFRLQAG VDPSELSART SSNLHKRTST QPYQLPSCGS VFRNPEPQKA GRLIEGLGLK
     GHRIGGAEVS TLHANFIVNT GNAQAADMDA LIRHVQAVVK QAHGLQLHPE VMRLGCFANS
     QAAAA
//

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