ID MURD_SODGM Reviewed; 438 AA.
AC Q2NVV3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE EC=6.3.2.9;
DE AltName: Full=D-glutamic acid-adding enzyme;
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
GN Name=murD; OrderedLocusNames=SG0447;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA Hattori M., Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights
RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT host.";
RL Genome Res. 16:149-156(2006).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AP008232; BAE73722.1; -; Genomic_DNA.
DR RefSeq; YP_454127.1; NC_007712.1.
DR ProteinModelPortal; Q2NVV3; -.
DR SMR; Q2NVV3; 3-438.
DR STRING; 343509.SG0447; -.
DR EnsemblBacteria; BAE73722; BAE73722; ENAG00097987.
DR GeneID; 3867422; -.
DR KEGG; sgl:SG0447; -.
DR PATRIC; 23647609; VBISodGlo61428_1128.
DR eggNOG; COG0771; -.
DR KO; K01925; -.
DR OMA; RCGELDV; -.
DR ProtClustDB; PRK03806; -.
DR BioCyc; SGLO343509:GJJC-472-MONOMER; -.
DR UniPathway; UPA00219; -.
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 ligase activity; 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:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00639; MurD; 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 PANTHER; PTHR23135:SF2; PTHR23135:SF2; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; Mur_ligase_C; 1.
DR SUPFAM; SSF53623; Mur_ligase_cen; 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 1 438 UDP-N-acetylmuramoylalanine--D-glutamate
FT ligase.
FT /FTId=PRO_0000257240.
FT NP_BIND 112 118 ATP (Potential).
SQ SEQUENCE 438 AA; 46714 MW; 7669E6BB5C343EFA CRC64;
MTDYRGEQVV IIGLGLTGLS CVDFLRRRGV TPRVMDTRFT PPGLEKLPAD VPRHLGSLHE
QWLLDATLIV TSPGVPLSHP ALAEAAAAGV AIIGDIELFA REASAPVVAI TGSNGKSTVT
CMVGEMAAAA GWQVGVGGNI GLPALTLLDS PCQLYVLELS SFQLETTHSL KAAAATVLNI
SEDHMNRYPL GLQQYRAAKL KIYHDAAVCV VNAEDALTLP VRGHDARCIS FGAERGDYCL
RRHAGQTWLM ARGEPLLEGA ELRVGGRHNY TNALAALALS DALGIPSAAS LAALRQFRGL
THRFELVHER RGVRWINDSK ATNVGSTEAA LNGLEVVGTL HLLLGGDGKS ADFTPLTPWL
QGDRVQLYCF GQDGAQLASL CPEAATLTET LEQAMRIIGS RVRAGDLVLL SPASASLDQF
SNFEVRGDVF TRLAREVG
//
