ID A0A1L2ZKJ5_9MICC Unreviewed; 511 AA.
AC A0A1L2ZKJ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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};
DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639};
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:APF39730.1};
GN ORFNames=BHE16_00390 {ECO:0000313|EMBL:APF39730.1};
OS Neomicrococcus aestuarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Neomicrococcus.
OX NCBI_TaxID=556325 {ECO:0000313|EMBL:APF39730.1, ECO:0000313|Proteomes:UP000183530};
RN [1] {ECO:0000313|EMBL:APF39730.1, ECO:0000313|Proteomes:UP000183530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18 {ECO:0000313|EMBL:APF39730.1,
RC ECO:0000313|Proteomes:UP000183530};
RA Luo Y.;
RT "Genome sequencing of Zhihengliuella aestuarii B18 antagonistic to
RT Plasmodiophora brassicae.";
RL Submitted (NOV-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}.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00639}.
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DR EMBL; CP018135; APF39730.1; -; Genomic_DNA.
DR RefSeq; WP_071893204.1; NZ_CP018135.1.
DR AlphaFoldDB; A0A1L2ZKJ5; -.
DR STRING; 556325.BHE16_00390; -.
DR KEGG; nae:BHE16_00390; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000183530; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR000960; Flavin_mOase.
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 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 Pfam; PF21799; MurD-like_N; 1.
DR PRINTS; PR00370; FMOXYGENASE.
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.
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_00639}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639};
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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639};
KW Reference proteome {ECO:0000313|Proteomes:UP000183530}.
FT DOMAIN 142..326
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 348..415
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 432..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 511 AA; 54144 MW; 98F2759AC1C657A0 CRC64;
MACWTVTNLD ELTSWDADWK GVRVLVTGLG VTGFSVADTL IELGATVVVV DGSMSELVAQ
RADTLKIVGA HDVLLGSEHL DSLPLIDGAQ PDVVVTSPGW NPRHPVLAAA TEAGIPIWGD
IEVAWRVRER AGRTPAEWLV LTGTNGKTTT VEMTASILRA AGKRAIAVGN VGTPILDAIR
DPQGYDVFAI ELSSFQLHYT HTISPLASAV LNLAEDHVDW HGSIEEYFAA KAKIYERTRA
AVIYNVEQRE TEKMVEEADV VDGCRAIGFT TGIPGLSMLG VVEGLLVDRA FIEERRSSAA
ELASLSDLGE IVPQHTAANA LAAAALCRAY GVSAAAVKQG LSDFEPGDHR IQVIGSKDGV
TWINDSKATN PHAASASLSA FKPIVWVAGG LPKGVEYDEL VLKHRERLRA VVLIGADSSK
LAESLARHAP DVPVIGPGVQ ETGSEATEQG SVEQRSSSGE DVMRQAVAAA ASVAQDGDTV
LMAPAAASMD QFQSYAHRGN AFVQAVQDLL R
//
