ID MURD_FUSNN Reviewed; 432 AA.
AC Q8RDQ1;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 27-NOV-2024, entry version 138.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639};
GN Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; OrderedLocusNames=FN1458;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate + ATP =
CC UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + ADP + phosphate
CC + H(+); Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378, ChEBI:CHEBI:29986,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83898,
CC ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00639};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00639}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL95651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009951; AAL95651.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_604352.1; NC_003454.1.
DR RefSeq; WP_029597345.1; NZ_CP084110.1.
DR AlphaFoldDB; Q8RDQ1; -.
DR SMR; Q8RDQ1; -.
DR STRING; 190304.FN1458; -.
DR PaxDb; 190304-FN1458; -.
DR EnsemblBacteria; AAL95651; AAL95651; FN1458.
DR GeneID; 79784421; -.
DR KEGG; fnu:FN1458; -.
DR PATRIC; fig|190304.8.peg.2018; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_0_0_0; -.
DR InParanoid; Q8RDQ1; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-UniRule.
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; IPR036565; Mur-like_cat_sf.
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; PF08245; Mur_ligase_M; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..432
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109017"
FT BINDING 98..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ SEQUENCE 432 AA; 49390 MW; 558689D931A3E0A3 CRC64;
MKKAMIYGLG ISGTGAKELL EKEGYKIIVV DDKKAMTSEE ALNHLEGLEF FIKSPGIPYN
DFVKEVQKRG IKILDEIEIA YNYMIEKGLK TKIIAITGTN GKSTTTAKIS DMLNHAGYKA
TYAGNIGRSL SEVLLKEKDL DFISLELSSF QLENIENFKP CISMIINIGP DHIERYKSFD
EYYNTKFNIT KNQTEDLYFI ENIDDEEIEK RAKQIKAKRI SVSKFKKADI FVENDKIYHD
KDDIIDVDKL SLKGIHNLEN TLFMVATAEI LKLDREKLKE FLMIATPLEH RTELFFNYGK
LKFINDSKAT NVDSTKFAIQ ANKNSILICG GYDKGVDLAP LAEMIKENIK EVYLIGVIAD
KIENELKKVG YEDNKIHKLV NIENSLQDMR KRFTKDSDEV ILLSPATSSY DQFNSFEHRG
KVFKELVLKI FG
//
