ID R6UD32_9CLOT Unreviewed; 464 AA.
AC R6UD32;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639};
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=BN818_01669 {ECO:0000313|EMBL:CDC82420.1};
OS Clostridium sp. CAG:964.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262848 {ECO:0000313|EMBL:CDC82420.1, ECO:0000313|Proteomes:UP000018136};
RN [1] {ECO:0000313|EMBL:CDC82420.1, ECO:0000313|Proteomes:UP000018136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:964 {ECO:0000313|Proteomes:UP000018136};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639}.
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:CDC82420.1}.
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DR EMBL; CBFZ010000088; CDC82420.1; -; Genomic_DNA.
DR AlphaFoldDB; R6UD32; -.
DR STRING; 1262848.BN818_01669; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000018136; 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: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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00639}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639};
KW Reference proteome {ECO:0000313|Proteomes:UP000018136}.
FT DOMAIN 121..298
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT BINDING 123..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 464 AA; 51033 MW; D21EEE5D0BCB0768 CRC64;
MDKRIENFFK SMNGKKIAFC GIGTSNLPLI ELFIKYGASV TACDRRTREQ LGDSADVAQK
AGAKLSLGDD YLKNLDVDIV FRTPGMRYYM DELVEMRNRG VVVTSEMEVF FDLCPCKIYA
ITGSDGKTTT TSIIAQMLQA QGKTVHLGGN IGKPLLPEIE SIGYDDAAVV ELSSFQLISM
RKGPDVAVVT NLAPNHLDIH KDMQEYIDAK KNLVIHQGAF SRVVLNKDNE ITNGFEPECR
GRVLKFSRKS QLNNGAYLDE NNNIVFADNG KKTIVMNIAD IKIPGMHNVE NYMAAISAVW
GEVSVENIVN VAKTFAGVEH RAEFVREFEG VKYYNDSIAS SPTRTALGTL SLYDFKIILI
AGGYDKKIPY DGLGPVICDK VKYLILMGAT APKIKAAVLN ADNYSDGNPT IIEVSNMEEA
VAKAREVAKP GDLVSMSPAS ASFDLYKNFD QRGKHFKSIV NGLK
//
