(data stored in ACNUC7421 zone)

SWISSPROT: MURD_PARDP

ID   MURD_PARDP              Reviewed;         466 AA.
AC   A1AZK7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   13-FEB-2019, entry version 82.
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};
GN   OrderedLocusNames=Pden_0589;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to 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-
CC         alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate; Xref=Rhea:RHEA:16429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29986, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83898, ChEBI:CHEBI:83900,
CC         ChEBI:CHEBI:456216; EC=6.3.2.9; Evidence={ECO:0000255|HAMAP-
CC         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; CP000489; ABL68701.1; -; Genomic_DNA.
DR   RefSeq; WP_011746934.1; NC_008686.1.
DR   SMR; A1AZK7; -.
DR   STRING; 318586.Pden_0589; -.
DR   PRIDE; A1AZK7; -.
DR   EnsemblBacteria; ABL68701; ABL68701; Pden_0589.
DR   KEGG; pde:Pden_0589; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049428; -.
DR   KO; K01925; -.
DR   OMA; VDKGNDY; -.
DR   BioCyc; PDEN318586:G1GW1-597-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZK7.
DR   SWISS-2DPAGE; A1AZK7.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis;
KW   Reference proteome.
FT   CHAIN         1    466       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000301444.
FT   NP_BIND     127    133       ATP. {ECO:0000255|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   466 AA;  49334 MW;  F2ECF4F0853E09A9 CRC64;
     MIPVQGVQNQ TIAVLGLGRS GRATAAALAA GGARVVAWDD GVDTREQAEQ EGLHLLDLTQ
     DQNWDGISAL IASPGIPHLY PKPHPVIARA YALGVPVDND IGLFFRSFAT AEWERFDTTP
     RVIAVTGSNG KSTTTALIHH ILKETGRPTQ IGGNIGTGVL SLDPAHDGEV VVLELSSYQT
     DLARALTPDV AVFTNLSPDH LDRHGGLGGY FAAKRRLFAE GGPDRAVIGV DEVEGRYLAG
     QLGMGAADDR VIRVSSGQKL EGFGWSVFAR KGYLAEYRKG RQVASIDLRG IQGLPGAHNH
     QNACAAYAAA RAVGIAPREI ERAFHSFQGL PHRSQTVAEI GGVAWVNDSK ATNVDAAAKA
     LAAFPRIRWI AGGMGKDGGI EALAPCLGPV VKAYLIGHSA RDFALQIGQT PYEIVETMEQ
     AVARAAAEAQ PGETVLLAPA AASFDQYPNF EKRGEHFTAL VKALQA
//

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