ID   MURB_SYNE7              Reviewed;         301 AA.
AC   P95837; Q31ME9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 3.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase;
DE            EC=1.3.1.98;
DE   AltName: Full=UDP-N-acetylmuramate dehydrogenase;
GN   Name=murB; OrderedLocusNames=Synpcc7942_1740;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kirzner S., Kaplan A.;
RT   "Cyanobacterial mutants capable of growing in the presence of high
RT   concentration of zinc.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB47523.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U86147; AAB47523.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000100; ABB57770.1; -; Genomic_DNA.
DR   RefSeq; WP_011244661.1; NC_007604.1.
DR   AlphaFoldDB; P95837; -.
DR   SMR; P95837; -.
DR   STRING; 1140.Synpcc7942_1740; -.
DR   PRIDE; P95837; -.
DR   EnsemblBacteria; ABB57770; ABB57770; Synpcc7942_1740.
DR   KEGG; syf:Synpcc7942_1740; -.
DR   eggNOG; COG0812; Bacteria.
DR   HOGENOM; CLU_035304_1_1_3; -.
DR   OMA; MQNIGAY; -.
DR   OrthoDB; 841869at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1740-MON; -.
DR   UniPathway; UPA00219; -.
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.
FT   CHAIN           1..301
FT                   /note="UDP-N-acetylenolpyruvoylglucosamine reductase"
FT                   /id="PRO_0000179277"
FT   DOMAIN          24..190
FT                   /note="FAD-binding PCMH-type"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        220
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   CONFLICT        150
FT                   /note="V -> E (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="T -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="A -> P (in Ref. 1; AAB47523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="L -> V (in Ref. 1; AAB47523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="G -> R (in Ref. 1; AAB47523)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  32347 MW;  3467F981792452E4 CRC64;
     MTGAVSLLET LQQAVPLAGF TSFRVGGLAQ FYDEPASVEA IATAWQWARL ADFPVTFLGA
     GSNLLISDRG LPGLVLNLRR LQGATFDLAT GCVEVAAGEP IPRLAWAAAR QGWSGLEWAV
     GIPGTLGGAV VMNAGAQGGC MADILQSVQV ITDQGLETWS REQLQYDYRH SVLQTGHACV
     VSAQLQLQPG FERSQVLTTT STNFRQRKRT QPYHLPNCGS VFRNPEPQKA GQLIEACGLK
     GYQIGDAQVS ELHANFILNC GAARAQDILS LIRHVQGTVG DHFGVNLHPE VKLLGEFQDV
     I