ID A0A0Q8EWE2_9GAMM Unreviewed; 467 AA.
AC A0A0Q8EWE2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_02208};
DE EC=6.3.2.53 {ECO:0000256|HAMAP-Rule:MF_02208};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_02208};
DE Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000256|HAMAP-Rule:MF_02208};
GN Name=murD {ECO:0000313|EMBL:KRA51763.1};
GN Synonyms=murD2 {ECO:0000256|HAMAP-Rule:MF_02208};
GN ORFNames=ASD72_01315 {ECO:0000313|EMBL:KRA51763.1};
OS Pseudoxanthomonas sp. Root630.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA51763.1, ECO:0000313|Proteomes:UP000051081};
RN [1] {ECO:0000313|EMBL:KRA51763.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA51763.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA51763.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA51763.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC {ECO:0000256|HAMAP-Rule:MF_02208}.
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {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|RuleBase:RU003664};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC EC=6.3.2.53; Evidence={ECO:0000256|HAMAP-Rule:MF_02208};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_02208,
CC ECO:0000256|RuleBase:RU003664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_02208, ECO:0000256|RuleBase:RU003664}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02208}.
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:KRA51763.1}.
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DR EMBL; LMGY01000001; KRA51763.1; -; Genomic_DNA.
DR RefSeq; WP_056878165.1; NZ_LMGY01000001.1.
DR AlphaFoldDB; A0A0Q8EWE2; -.
DR STRING; 1736574.ASD72_01315; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051081; 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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-EC.
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 HAMAP; MF_02208; MurD2_subfam; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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 InterPro; IPR043687; MurD2.
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; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02208};
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02208,
KW ECO:0000256|RuleBase:RU003664};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02208,
KW ECO:0000256|RuleBase:RU003664};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02208,
KW ECO:0000256|RuleBase:RU003664};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02208,
KW ECO:0000256|RuleBase:RU003664};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02208};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02208};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02208};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02208,
KW ECO:0000256|RuleBase:RU003664}.
FT DOMAIN 120..289
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 311..383
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02208"
SQ SEQUENCE 467 AA; 49593 MW; 058C2CD2F4D19781 CRC64;
MRISQLEGRR VALWGWGREG RAAHHAVRAR LPSLPLTLFC NAQEAADAAA LGDPLLAVET
VATAERLSAF DIVIKSPGIS PNTPVAVAAS GAGTRFIGGT GLWFAEHAGE DGVVAHTFCV
TGTKGKSTTT SLLAHLLRAA GRRTVLAGNI GLPMLEVLDP QPVPDEWAIE LSSYQTGDVA
DSGARPDVAI VLNLFPEHLD WHGSEARYIA DKLKLVTGAH PRIAVLNAAD PRLAALDLPH
SDVRWFNRAD GWHLREDDLY RGDVFVMDTR PLPLPGRHNR SNLCAVLTAL EARGIDALPL
VAHAQSFRPL PNRLQAMGAR DGITWVNDSI STTPHATLAA LECFAGRRIA LLVGGHDRGV
DWSDFAAHMR EDAPATIITM GANGPRIHAL LAPVAREAGF TLIGVETLPE AIAAAREALG
DEGVVLLSPG APSFGQYRDY VARGRNFAEL AGFDPDAITS IPGLGAG
//
