ID A0A1E5MN67_9MICO Unreviewed; 509 AA.
AC A0A1E5MN67;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN Name=murD {ECO:0000256|HAMAP-Rule:MF_00639};
GN ORFNames=Cus16_0690 {ECO:0000313|EMBL:OEI70069.1};
OS Curtobacterium sp. ER1/6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI70069.1, ECO:0000313|Proteomes:UP000095245};
RN [1] {ECO:0000313|EMBL:OEI70069.1, ECO:0000313|Proteomes:UP000095245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER1/6 {ECO:0000313|EMBL:OEI70069.1,
RC ECO:0000313|Proteomes:UP000095245};
RA Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA Araujo W.L.;
RT "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT strain isolated from Citrus sinensis with potential to be used as a
RT biocontrol agent.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00639,
CC ECO:0000256|RuleBase:RU003664};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639,
CC ECO:0000256|RuleBase:RU003664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00639}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEI70069.1}.
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DR EMBL; MJAK01000001; OEI70069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5MN67; -.
DR STRING; 1891920.Cus16_0690; -.
DR PATRIC; fig|1891920.3.peg.718; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000095245; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00639; MurD; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005762; MurD.
DR NCBIfam; TIGR01087; murD; 1.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00639};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00639};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW ECO:0000256|RuleBase:RU003664};
KW Reference proteome {ECO:0000313|Proteomes:UP000095245}.
FT DOMAIN 136..328
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 351..418
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 138..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 509 AA; 53443 MW; 2CC54738B121404A CRC64;
MSADARLDGL DSWYAEGWKG LRVAVLGLGS TGFSVADTLV ELGSEVTVHA PDGPDDTVEL
LDVIGARFER TSLDTVPGSL VAQAPDLVVV SPGLPPHNAS VQWATANSVV WGDIELAWRV
RDKVVRGPIA APWVTITGTN GKTTTTQLTT AMFAASGLRA VACGNIGVPV LDVVRDPEGF
DVLVVELSSH QLHYMPTTGD GAVVPLASAC LNIADDHLEW HGSAEDYRAA KAKVYERSVM
ACVYNTADDA TRRMVEQADV VEGCRAVGFT PGVPAPGDVG IVDDVLCDRA FTEDRRNSAL
ELATLADLEQ AGLASPHMTM NVLAAAALAR AASVAPAHIR SAVQGFRADH HRTEHVATAD
GITWVDDSKA TNPHAATASL ASFETVVWIV GGQFKGVDID GLVERFGPDA RAVVVIGTDR
APVLEAFARH APGVPVLQVE ATDTEHVMPE AVRHAASVAR PGDTVLLAPA AASFDQFGSY
ADRGRRFAAA VHEHLGGTAD GDHGSPERP
//
