ID A0A6N4QZC8_BLAVI Unreviewed; 481 AA. AC A0A6N4QZC8; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 25-MAY-2022, entry version 6. 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=DI628_07095 {ECO:0000313|EMBL:TKW60658.1}; OS Blastochloris viridis (Rhodopseudomonas viridis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Blastochloridaceae; Blastochloris. OX NCBI_TaxID=1079 {ECO:0000313|EMBL:TKW60658.1, ECO:0000313|Proteomes:UP000320948}; RN [1] {ECO:0000313|EMBL:TKW60658.1, ECO:0000313|Proteomes:UP000320948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2_018_000_R2_106 {ECO:0000313|EMBL:TKW60658.1}; RX PubMed=28232747; DOI=.1038/s41467-016-0009-6; RA Bhardwaj A., Kaur J., Wuest M., Wuest F.; RT "In situ click chemistry generation of cyclooxygenase-2 inhibitors."; RL Nat. Commun. 8:1-1(2017). 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:TKW60658.1}. 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; VAFM01000002; TKW60658.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000320948; 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: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; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00208; MurE; 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; IPR035911; MurE/MurF_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:TKW60658.1}; 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 97..302 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 323..409 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 99..105 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 401..404 FT /note="Meso-diaminopimelate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOTIF 401..404 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 24 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 171 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 179 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 377 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 453 FT /note="Meso-diaminopimelate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 457 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 211 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 481 AA; 50553 MW; 7F2169946E261749 CRC64; MKFSEIVGQP VAADFAVQNV CDDTRKLAAG DVFVWDSRVA PKQDVAALVA DAKAKGATAI VTDVPVDGAV QVTNAGEVLS RFAALRWPEQ PPVMLGVTGT SGKTSVVWFG RQLAQLSGVN AASVGTLGVM RKDEDVETEY TGFTSPNALK IGPILQTLAR EKVQTCLLEV SSHALVLNRV DAVKFTAAGL TNITQDHLDF HGDLAEYHAA KLRLFAEVLP EDGTAVLNIG RMETLPAASV AKQRGCRVLT VGTANAELVA EVVEANGRGL QLNLKYDSVP VPVHVPLIGT FQAENLAVAL GLLVGSGHDW KKISGAVSRM TAVPGRMEVV KSAPTQPSVV VDYAHKPDAL QRALESLRPV VKGGGKLRVV FGCGGNRDAT KRPIMGRIAA ELADVVYVTD DNPRKENAAD IRQQVLAGVT AGGAKGLEFD DRKAAIAAAI ADGGPDDVVL IAGKGHESGQ IVGDEVHPFD DRLVAREVLG G //