ID   MURD_ANAVT              Reviewed;         455 AA.
AC   Q3MF19;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
DE   AltName: Full=D-glutamic acid-adding enzyme;
GN   Name=murD; OrderedLocusNames=Ava_0793;
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: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; CP000117; ABA20417.1; -; Genomic_DNA.
DR   RefSeq; YP_321312.1; -.
DR   GeneID; 3680732; -.
DR   GenomeReviews; CP000117_GR; Ava_0793.
DR   KEGG; ava:Ava_0793; -.
DR   NMPDR; fig|240292.3.peg.2586; -.
DR   HOGENOM; Q3MF19; -.
DR   OMA; Q3MF19; IRSFAGM.
DR   BioCyc; AVAR240292:AVA_0793-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate lig...; IEA:HAMAP.
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_00639; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01087; murD; 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    455       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000257164.
FT   NP_BIND     112    118       ATP (Potential).
SQ   SEQUENCE   455 AA;  49411 MW;  BC47CCF630D44A46 CRC64;
     MSKAHVVGLG KSGVAAARLL KREGWEVVLS DRNTSDTLLK QQQELAKEQI TVELGYSLDF
     AGALPDLIVV SPGVPWDIPA LVKARELGIE TIGEMELAWR HLKSLPWVGI TGTNGKTTTT
     ALIAAIFQAA GFDAPACGNI GYAACEVALA ATPPDWIIGE MSSYQIESSL TLAPHISIWT
     TFTPDHLARH KTLENYYDIK AKLLRQSHLQ VFNGDDAYLS KIGASHWPDA YWTSVKGKDY
     LIGDKGFYIE DGWVVEQLQP NSSPQRIVAA EALRMVGAHN LQNLLMAVAA ARLADIPPNA
     IDKAVREFPG VAHRLEHICT WQGIDFINDS KATNYDAAEV GLASVKSPVI LIAGGEAKPG
     DDAAWLAKIQ GQTSAVLLIG NAAPAFAQRL QEIGYSNYEI VETMEQAVRR SLDLAKHHQA
     PVVLLSPACA SFDQYPNFEA RGDHFRQLCL ELVGS
//