ID   MURE_ANAVT              Reviewed;         496 AA.
AC   Q3ME15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
DE            EC=6.3.2.13;
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
DE   AltName: Full=Meso-diaminopimelate-adding enzyme;
DE   AltName: Full=Meso-A2pm-adding enzyme;
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase;
GN   Name=murE; OrderedLocusNames=Ava_1147;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-
CC       N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-
CC       heptanedioate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family. MurE subfamily.
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DR   EMBL; CP000117; ABA20771.1; -; Genomic_DNA.
DR   RefSeq; YP_321666.1; -.
DR   GeneID; 3683401; -.
DR   GenomeReviews; CP000117_GR; Ava_1147.
DR   KEGG; ava:Ava_1147; -.
DR   NMPDR; fig|240292.3.peg.1672; -.
DR   HOGENOM; Q3ME15; -.
DR   OMA; Q3ME15; FPVIVDY.
DR   BioCyc; AVAR240292:AVA_1147-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-...; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00208; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    496       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012335.
FT   NP_BIND     116    122       ATP (Potential).
FT   REGION      158    159       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      413    416       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       413    416       Meso-diaminopimelate recognition motif.
FT   BINDING      32     32       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     185    185       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     191    191       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     193    193       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     389    389       Meso-diaminopimelate (By similarity).
FT   BINDING     464    464       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     468    468       Meso-diaminopimelate (By similarity).
FT   MOD_RES     225    225       N6-carboxylysine (By similarity).
SQ   SEQUENCE   496 AA;  53416 MW;  DCDF7907B96B79BA CRC64;
     MKLRELLATV DSVENLPPVL ADTEVKGIKT NSHACGAGDL FIGMPGTRVD GGEFWPSAIA
     SGAIAAIVSP QAVEKNPPSD EAVVISSNNM TKACAAIAAA FYGYPGQKLK LVGVTGTNGK
     TTTTHLIEFF LTKAQLSTAL MGTLYTRWPG FEQTATHTTP FAVELQQQLA QAVNAGCEFG
     VMEVSSHALA QGRVLGCPFE VGVFSNLTQD HLDYHSDMED YFAAKALLFS PDYLKGRAII
     NADDTYGQRL IKALSPEKVW SYSVNDSSAD LWMSDLSYEP NGVTGTIHTP EGDVSFRSPL
     VGQYNLENLL ASVGAVLHLG LDLQLIANAI PEFPGVPGRM ERVQINPDQD ISVIVDYAHT
     PDSLENLLKA ARPFIPGRMI CVFGCGGDRD RTKRPKMGKI AAELADLAFV TSDNPRTEDP
     EKILDDILAG IPDTVQPTVI GDRAIAIRTA ILQAQPGDGV LLAGKGHEDY QILGTEKIHF
     DDREHARAAL TEREKL
//