ID A0A417HSY0_9CLOT Unreviewed; 477 AA. AC A0A417HSY0; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-MAY-2023, entry version 20. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208}; GN ORFNames=DW742_07290 {ECO:0000313|EMBL:RHT76235.1}; OS Butyricicoccus sp. AM28-25. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Butyricicoccus. OX NCBI_TaxID=2292294 {ECO:0000313|EMBL:RHT76235.1, ECO:0000313|Proteomes:UP000283242}; RN [1] {ECO:0000313|EMBL:RHT76235.1, ECO:0000313|Proteomes:UP000283242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM28-25 {ECO:0000313|EMBL:RHT76235.1, RC ECO:0000313|Proteomes:UP000283242}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) CC in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; CC EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135}. CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}. 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:RHT76235.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QUJL01000006; RHT76235.1; -; Genomic_DNA. DR AlphaFoldDB; A0A417HSY0; -. DR OrthoDB; 9800958at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000283242; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1. DR HAMAP; MF_00208; MurE; 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; IPR000713; Mur_ligase_N. DR InterPro; IPR035911; MurE/MurF_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1. DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1. DR Pfam; PF01225; Mur_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 SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1. DR TIGRFAMs; TIGR01085; murE; 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_00208}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00208}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:RHT76235.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00208}. FT DOMAIN 23..89 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 105..302 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 323..409 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT MOTIF 398..401 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 30 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 107..113 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 149..150 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 176 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 184 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 374 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 398..401 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 450 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 454 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 216 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 477 AA; 51813 MW; 41048883E8BE34A1 CRC64; MKLQELLKNV AVKNSTAAQD IDIKEVRYDS RAVQPGDLFV AIRGYATDGH KYIAKAMEQG AAAVVCEEAP EGVPAVVVEN SRIALAEIAA NRFGHPAESM VMLGVTGTNG KTTTTYLVKH MLEDAGHKVG LIGTNQNLIG DEVIETERTT PESYELHALF ARMRDAGCTH VIMEVSSHSL VLDRVHGIPF AVGAFTNLTQ DHLDFHKTME EYRKAKALLF SISKKGVINL DDAAAEKMLA DAKCPCMTFS CGKPEADLEA TDLQLHADGV EFTAQYQGEK ADVKLPIPGH FSVENALTAL GIVLQLGMPL AAAAKSMATA TGVKGRVEVV PTDTDYTVLI DYAHSPDGVE NVLKAVRGFA KGRVVALFGC GGDRDRTKRP KMGKIAADLA DFCVVTSDNP RTEEPKAIID DILEGMKDSD TPMQVIVDRP EAIHWALAHA QKDDIIVLMG KGHETYQEVN HVKHHMDERE IVAEYFA //