ID Q0RNP3_FRAAA Unreviewed; 461 AA.
AC Q0RNP3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 61.
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=FRAAL2194;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Frankineae; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ60843.1; -; Genomic_DNA.
DR RefSeq; YP_712422.1; NC_008278.1.
DR ProteinModelPortal; Q0RNP3; -.
DR STRING; 326424.FRAAL2194; -.
DR GeneID; 4231936; -.
DR KEGG; fal:FRAAL2194; -.
DR PATRIC; 21914100; VBIFraAln347_2007.
DR eggNOG; COG0771; -.
DR HOGENOM; HOG000049429; -.
DR KO; K01925; -.
DR OMA; RCGELDV; -.
DR ProtClustDB; PRK01438; -.
DR BioCyc; FALN326424:GJ82-2161-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; 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 NP_BIND 125 131 ATP (By similarity).
SQ SEQUENCE 461 AA; 46576 MW; FA8326E501061A83 CRC64;
MASPAEPAGP RAWAGLSVLV VGVGVSGLAA ARALLARGAR VRVVDAGDTE RHRAAAADLR
ALGATVVLGG LPAGPGGAGL VVTSPGVPPT APLITGSAAA GVPVWGEVEL AWRWRGATRW
LAVTGTNGKT TTTEMLGAML AAGGRRAITA GNIGTPIVEA VAAEPPYDTL AVELSSFQLH
YTHTVAPLAA AVLNVAPDHL DWHGGAQAYA EAKARIWRDP ATIAIGNADD AASARLLAGA
PGRRVLFGRD PAARPAPGLT VEAGHLVDHA FGGGRLVAVR DLRVTGPHLI SNALAAAALA
RAEGVDPAAI GAALAEFRAG AHRNAEVAVI DGVRWVDDSK ATNPHAAAAS LAGYPSVVWI
AGGLNKGLAF DELVRDARGV LRGAVLIGRC ADEIAVALAR HAPDVPVERA AGMDDAVRAA
AALARAGDTV LLAPAAASMD MFRDYAARGD LFAEAVRARE G
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