(data stored in SCRATCH zone)

SWISSPROT: B8ICE7_METNO

ID   B8ICE7_METNO            Unreviewed;       460 AA.
AC   B8ICE7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382177};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382044};
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   OrderedLocusNames=Mnod_0493 {ECO:0000313|EMBL:ACL55535.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55535.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55535.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00382010}.
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
CC       + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC       alanyl-D-glutamate. {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382107}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00382165}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084461}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639, ECO:0000256|SAAS:SAAS00569906}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001349; ACL55535.1; -; Genomic_DNA.
DR   RefSeq; WP_015927245.1; NC_011894.1.
DR   ProteinModelPortal; B8ICE7; -.
DR   STRING; 460265.Mnod_0493; -.
DR   EnsemblBacteria; ACL55535; ACL55535; Mnod_0493.
DR   KEGG; mno:Mnod_0493; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049428; -.
DR   KO; K01925; -.
DR   OMA; VDKGNDY; -.
DR   OrthoDB; POG091H002Z; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Pfam; PF02875; Mur_ligase_C; 1.
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.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8ICE7.
DR   SWISS-2DPAGE; B8ICE7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084371};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459080};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084380};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084500};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459111};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084399};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084447, ECO:0000313|EMBL:ACL55535.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00459201};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    460       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002873946.
FT   DOMAIN      119    294       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      316    359       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     121    127       ATP. {ECO:0000256|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   460 AA;  47699 MW;  2AC084280DEE79CA CRC64;
     MTPSTTFAGR TLALFGLGGS GLATALSLQA GGARVVACDD NPERMAAAEA EGVATADLRG
     ADWAEFAALL LAPGVPFTHP EPHWTVKRAA SAGVPVIGDI ELFCRERATT APDAPFVAIT
     GTNGKSTTTA LIAHVLRETG HDVQMGGNIG TAILSLAPPA PGRVHVIEMS SFQIDLTPTL
     KPSVGVLLNI TPDHLDRHGD MANYAGIKER LIASSDHAVI GVDDDYTRAI AARHAGPLTR
     VHVGETAPGP GILARHGVLI DGCTEPPSPV ADLTGIPSLR GSHNWQNAGI AYAVARALGV
     APDAFAQALR SFPGLPHRME EVGRRGSVLF INDSKATNAD STEKALAAFP RVHWILGGKP
     KEGGIASLAP YFPRIAHAYL IGAASDAFAA TLEGHAPVSR CGTLEAAVAQ AAEDAAHEPE
     AVVLLSPACA SYDQFRSFED RGDQFRAMVR ALPGLVPTGG
//

If you have problems or comments...

PBIL Back to PBIL home page