ID A0A2G1XQJ8_STRCJ Unreviewed; 484 AA.
AC A0A2G1XQJ8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BLA24_00750 {ECO:0000313|EMBL:PHQ53493.1}, CYQ11_07760
GN {ECO:0000313|EMBL:PPT12798.1};
OS Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ53493.1, ECO:0000313|Proteomes:UP000222531};
RN [1] {ECO:0000313|EMBL:PHQ53493.1, ECO:0000313|Proteomes:UP000222531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ53493.1,
RC ECO:0000313|Proteomes:UP000222531};
RX PubMed=29053243;
RA Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT "Identification of the Biosynthetic Pathway for the Antibiotic
RT Bicyclomycin.";
RL Biochemistry 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:PPT12798.1, ECO:0000313|Proteomes:UP000239771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT12798.1,
RC ECO:0000313|Proteomes:UP000239771};
RA Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT bacterial classes.";
RL Submitted (DEC-2017) 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:PHQ53493.1}.
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DR EMBL; NHZO01000012; PHQ53493.1; -; Genomic_DNA.
DR EMBL; PKFQ01000001; PPT12798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1XQJ8; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000222531; Unassembled WGS sequence.
DR Proteomes; UP000239771; 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-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 CDD; cd01983; SIMIBI; 1.
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; 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 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};
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:UP000222531}.
FT DOMAIN 123..312
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 334..399
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 484 AA; 50319 MW; 2A10E1FA17DC768E CRC64;
MVGHQVSPAE FHGKHITVAG LGVSGVSAAR ALAGLGARVT VVDGGDGPAL RERARVLTDQ
GVAVRLGDAD TLPEGTDLVV TSPGWKPESP LFAAAAEAGV DVVGDVEIAW RLRGEDAAPW
LAVTGTNGKT TTVQMLASIL EAAGLRTAAV GNIGTPIIDV VLGDQPHDVL AVELSSYQLH
WAPSLRAHSA AVLNVAPDHL DWHGSMRAYA ADKGRIYEGN TVACVYNVED PRTEHLVREA
DVEEGCRAIG FTLGAPGPSM LGVVEGLLVD RAFVENRQQQ AQELAEVADI APSAGPAAPH
NIANALAAAA LARAFGVPPE AVRDGLRAFR PDAHRIAHVA EVDDVVYVDD SKATNPHAAQ
ASLATYESIV WIAGGLAKGA TFDELVTASA KRLRGVVLIG ADRALIREAL ARHAPDVPVV
DLDRTDTGAM AAAVREAARL AGPGDTVLMA PACASMDMFT NYNKRGEAFA EAVRALETGR
GADE
//