ID A0A9D5RKK9_9FIRM Unreviewed; 769 AA. AC A0A9D5RKK9; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 24-JAN-2024, entry version 4. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|HAMAP-Rule:MF_00208}; DE Includes: 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}; DE Includes: DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197}; DE AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197}; GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208}; GN Synonyms=dapF {ECO:0000256|HAMAP-Rule:MF_00197}; GN ORFNames=E7269_00350 {ECO:0000313|EMBL:MBE5921199.1}; OS Lachnospiraceae bacterium. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae. OX NCBI_TaxID=1898203 {ECO:0000313|EMBL:MBE5921199.1, ECO:0000313|Proteomes:UP000806229}; RN [1] {ECO:0000313|EMBL:MBE5921199.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SIG308 {ECO:0000313|EMBL:MBE5921199.1}; RA Peng X.; RT "Evolution of Biomass-Degrading Anaerobic Consortia Revealed by RT Metagenomics."; RL Submitted (APR-2019) 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 -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- CC lysine and an essential component of the bacterial peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, CC ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00197}; 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: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, 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 -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}. 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:MBE5921199.1}. 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; SVEO01000001; MBE5921199.1; -; Genomic_DNA. DR Proteomes; UP000806229; 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:0008837; F:diaminopimelate epimerase activity; 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:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. 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_00197; DAP_epimerase; 1. DR HAMAP; MF_00208; MurE; 1. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. 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 NCBIfam; TIGR00652; DapF; 1. DR NCBIfam; TIGR01085; murE; 1. 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; PF01678; DAP_epimerase; 2. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF54506; Diaminopimelate epimerase-like; 2. 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 PROSITE; PS01326; DAP_EPIMERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}; 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_00197}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00197}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00208}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}; 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..95 FT /note="Mur ligase N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 108..309 FT /note="Mur ligase central" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 329..410 FT /note="Mur ligase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02875" FT MOTIF 404..407 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT ACT_SITE 560 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10125" FT ACT_SITE 560 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 712 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" 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 110..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 151 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 152..153 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 179 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 187 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 380 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 404..407 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 456 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 460 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 496 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 551 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 561..562 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 652 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 685 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 703..704 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 713..714 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 654 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 703 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT MOD_RES 221 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 769 AA; 84898 MW; EFCA6B02CCDA00B2 CRC64; MLLKELLSEI TYEVLQGTTD TDVTELVYDS RKASVGCVFL CISGTTVDAH DFIPQVAEKG AAAIVVTKDV QVPANVTVVK VENARKALSY MAAAYFGKPA EKMTLIGITG TKGKTTTSYM VQAMLEMAGK KVGVIGTIGA VIDKGIVKTS NTTPESYEVQ RLFAKMVEAG CEYCIMEVSS QGMKMDRVAG VLFDYGIFTN FSSDHIGPNE HADMAEYLYC KSLLFRQCKV GIINRDSEYW QGVTEGHTCE LKTYGFDADA DLRGANQKLV RKSGVLGVEF DVEGVLNCHV KTCIPGRFSV YNCLTALAIG WHLDIPIEAM THALKNIRVP GRVELVDISP KFTIMVDYAH NAMSVESLLT TIKEYNPNRI ICVYGLGGNR SKVRRYEVGE LCGKMADLSV LTADNPRNEE IADIFNDIKI GLAKTNGKYI EIPDRKEAIY YAIDHAQEND IIVVFGKGHE DYQEIKGVRY PYNDKEAILS YLKREMNFVK LHGCGNPYIY MDVRGKNYEN AFLQALSIKV SDKSKGIGAD GLIVLDDAQT EGTDGRMRMF NADGSEGAMC GNGIRCLAKF MYEHAGIEKE HMVIETKSGL REVDLIHEGD EITKATVYMG HPEFEAANVP VISEHPVFMD GELPVELESG VKYCGTCMSM GNPHCVIFTE DIDALELAKI GPKFECHEMF PERVNTEFIE IVDRNNVRMR VWERGSGETM ACGTGACAVV AAGVRTGRLS NKVNVMMRGG TLEITYDVEN NDIYMTGEAV QICVGKLRV //