MURD_SHEVD
ID MURD_SHEVD Reviewed; 449 AA.
AC Q9F1N2; D4ZDU5;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SVI_4035;
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12153713; DOI=10.1093/oxfordjournals.jbchem.a003208;
RA Ishii A., Nakasone K., Sato T., Wachi M., Sugai M., Nagai K., Kato C.;
RT "Isolation and characterization of the dcw cluster from the piezophilic
RT deep-sea bacterium Shewanella violacea.";
RL J. Biochem. 132:183-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12;
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
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=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: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=BAJ04006.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB052554; BAB19200.1; -; Genomic_DNA.
DR EMBL; AP011177; BAJ04006.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041420110.1; NC_014012.1.
DR AlphaFoldDB; Q9F1N2; -.
DR SMR; Q9F1N2; -.
DR STRING; 637905.SVI_4035; -.
DR EnsemblBacteria; BAJ04006; BAJ04006; SVI_4035.
DR KEGG; svo:SVI_4035; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_1_0_6; -.
DR OMA; CNFENYL; -.
DR OrthoDB; 1093223at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002350; 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: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_00639; MurD; 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; IPR005762; MurD.
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 TIGRFAMs; TIGR01087; murD; 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..449
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109080"
FT BINDING 116..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ SEQUENCE 449 AA; 47783 MW; 0DA48359766B05C5 CRC64;
MELDNSHLVL GLGATGLSVV RYLCRQGITP LVMDSRDQPP GAEQLALEFP EVNLITGGFD
CRYLVQASQI VISPGIAIDT PEIRAAIDMD IEVIGDVELF ARAIKDRSPC VIGITGSNGK
STVTTLVGEM AKAAGLNYAV GGNIGIPVLD LLQKPVDLYI LELSSFQLET THSLNCISAT
CLNISEDHMD RYSDLEAYRQ AKLALYDQSK RALFNREDSL TQPNDPMNQN SFGLTSPVND
EWGVKDGKIV HGTTEIASLQ DVAIVGSHNH ANLIAAMALA YHAGIDKEPM IQVAKNFTGL
AHRCELVANI AAVAYVNDSK ATNVGATVAA LEGLGEHLGD IILIVGGDGK GADFTPLETV
FNKVAHLITL GKDGDKIAAL KEHSHKADSM ADAVKQAAEL ATAGDIVLLS PACASLDMYK
NFMARGDDFR QLAQALSVET LDSEASADV
