ID   MURD_BURP1              Reviewed;         504 AA.
AC   Q3JND6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 32.
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=BURPS1710b_3547;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Woods D.E., Nierman W.C.;
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; CP000124; ABA48716.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_334917.2; -.
DR   GeneID; 3688229; -.
DR   GenomeReviews; CP000124_GR; BURPS1710b_3547.
DR   KEGG; bpm:BURPS1710b_3547; -.
DR   TIGR; BURPS1710b_3547; -.
DR   HOGENOM; Q3JND6; -.
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    504       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000257171.
FT   NP_BIND     129    135       ATP (Potential).
SQ   SEQUENCE   504 AA;  52549 MW;  5F5BD80F4EB8C5D7 CRC64;
     MFGDRQRPMV LVLGLGESGL AIARWCARHG CRLRVADTRE TPPNLAALTA AGVDFEFVGG
     AFSPALVDGG IELVALSPGL SPLAEDLAPL VAAARERGIP VWGELEFFAQ ALAALGANGY
     APKVIAITGT NGKTTTTSLA GLLCERAGKK VAVAGNISPA MLDKLTEAID AAALPDVWVL
     ELSSFQLDTA HTFAPDAATI LNITQDHLDW HGGFAAYAAA KGRVFGPRTV RVLNRDDAEV
     MRFAPPAAAA DAPRAVTFGL NEPAADGDYG LLRENGIAWL VEAIDRDGAD APAAPSRRRK
     QEAANPPDIA LKRLMPADAL RIRGLHNAAN ALAAYALARA IGLPAAPLLH GLREYRGEPH
     RVEVIATLDG VDYVDDSKGT NVGATVAALD GLAQRAVLIA GGDGKGQDFE PLAAPVARWC
     RAVMLIGRDA PALREALADT GVPLADHATL EAAVRAASAL AQPGDAVLLS PACASLDMFR
     NYAHRADVFR SAVEDIALEK GTTL
//