(data stored in ACNUC7421 zone)

SWISSPROT: MURD_ALCBS

ID   MURD_ALCBS              Reviewed;         441 AA.
AC   Q0VS04;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 88.
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=ABO_0596;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
DR   EMBL; AM286690; CAL16044.1; -; Genomic_DNA.
DR   RefSeq; WP_011587882.1; NC_008260.1.
DR   SMR; Q0VS04; -.
DR   STRING; 393595.ABO_0596; -.
DR   PRIDE; Q0VS04; -.
DR   EnsemblBacteria; CAL16044; CAL16044; ABO_0596.
DR   KEGG; abo:ABO_0596; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049427; -.
DR   KO; K01925; -.
DR   OMA; CSSFDMF; -.
DR   OrthoDB; 1093223at2; -.
DR   BioCyc; ABOR393595:ABO_RS03080-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008871; 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; UDP-N-AcMur-Glu_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   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0VS04.
DR   SWISS-2DPAGE; Q0VS04.
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..441
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000257163"
FT   NP_BIND         113..119
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   441 AA;  46537 MW;  C5CDE451C470EE39 CRC64;
     MAKDGFDLVI GLGVTGRSVI RYLTDQGMPV RAIDTRAEPV GLDALCADFP DLKVHTGGFK
     KGWMGKARRL IVSPGVAVST PAIAEQVVDG KEVIGDIELF ARAASEPLVA ITGSNAKSTV
     TTLLGQVADA CGMNPGIGGN LGVPALELLD DQARLYVLEL SSFQLETTYS LSAEVATVLN
     VSQDHLDRYA SFADYLAAKQ RVYDGCQVAV WNRDDLATRP PATVARQISF GAHPEADYRL
     DSENGQLLCR GEPLLSLSEL ALTGHHNAMN ILSVLAISDA LSLNRDKALA TVKTFTGLPH
     RCQLVAESGG VRWFNDSKAT NVGATLAALT GIGESIEGKV ILVAGGLGKG QDFSPLAEPA
     RQYLRAALLM GEDRTTVAQG MSAAPCELVA DMAVAVRRAH ALAQPGDAVL LSPACASFDQ
     YSGFAARGDD FTTRAQELCH D
//

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