ID A0A1A9GLD4_9ACTN Unreviewed; 489 AA.
AC A0A1A9GLD4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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 ECO:0000313|EMBL:ANH39147.1};
GN ORFNames=I601_2731 {ECO:0000313|EMBL:ANH39147.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH39147.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH39147.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH39147.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-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}.
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DR EMBL; CP015079; ANH39147.1; -; Genomic_DNA.
DR RefSeq; WP_068114937.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GLD4; -.
DR STRING; 1300347.I601_2731; -.
DR KEGG; ndk:I601_2731; -.
DR PATRIC; fig|1300347.3.peg.2726; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000077868; Chromosome.
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:UP000077868}.
FT DOMAIN 130..314
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 337..402
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 132..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 489 AA; 51380 MW; 79D161FDFEB3C70E CRC64;
MSAPRDLDGL DQTSSWDGVR AVVAGFGVSG FAAADNLNHL GAAVTALDES ATGKEEKAEL
LEVLGATITL GPGATARLPD DVDVVVTSPG WRPDSPLLVQ ARDRGVPVWG EVELAWRLRH
PEHAAPWLAV TGTNGKTTTV QMLDAILRAA GLRSVAAGNV GLPIVEAVMD PTPYDVLAVE
LSSFQLHYTS SMSAESAVVL NVAEDHLDWY PSMSEYAADK GRVYERVQRA CVYNVADPVT
EELVRAADVV EGARAVGFTL GMPGVGMLGL VEDILVDRAF IEQRTDSAAE LVTVGELASS
APHYVANALA AAALARAHGV SQQAVRDGLR AFRPDGHRIA EVARHDDVTW VDDSKATNPH
AALASLRAYD SVVWVAGGLA KGARFEELVA AVRDRLRGVV LLGRDRHVVA EALARHAPDV
PVIDVGADET GVTDDEHAPM GRVVEAAAGL AQPGDTVLLA PGCASQDMFT DYGARGDAFA
AAVRARTGP
//
