(data stored in ACNUC7421 zone)

HOGENOM: STRM5_1_PE1013

ID   STRM5_1_PE1013                       STANDARD;      PRT;   469 AA.
AC   STRM5_1_PE1013; B4SN73;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase; EC=6.3.2
DE   9;AltName: Full=D-glutamic acid-adding enzyme;AltName:
DE   Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
DE   (STRM5_1.PE1013).
GN   Name=murD; OrderedLocusNames=Smal_1013;
OS   STENOTROPHOMONAS MALTOPHILIA R551-3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=391008;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STRM5_1.PE1013.
CC       Stenotrophomonas maltophilia R551-3 chromosome, complete genome.
CC       chromosome 1, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B4SN73_STRM5
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MurCDEF family.
CC   -!- SIMILARITY: Belongs to the murCDEF family.
CC   -!- GENE_FAMILY: HOG000049428 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4SN73; -.
DR   EMBL; CP001111; ACF50718.1; -; Genomic_DNA.
DR   RefSeq; YP_002027401.1; NC_011071.1.
DR   ProteinModelPortal; B4SN73; -.
DR   STRING; B4SN73; -.
DR   GeneID; 6478368; -.
DR   GenomeReviews; CP001111_GR; Smal_1013.
DR   KEGG; smt:Smal_1013; -.
DR   OMA; DQFSSYK; -.
DR   ProtClustDB; PRK04690; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00639; MurD; 1; -.
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   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23135:SF2; PTHR23135:SF2; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; Mur_ligase_C; 1.
DR   SUPFAM; SSF53623; Mur_ligase_cen; 1.
DR   TIGRFAMs; TIGR01087; MurD; 1.
DR   HOGENOMDNA; STRM5_1.PE1013; -.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   469 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKISKFEGKR VALWGWGREG RAAFAVLHSR LPTLGLSLFC PAAEVEAARA ETHGALDVRG
     EPSAETLAAF DVVIKSPGIS PYQPIALAAA AQGTTFIGGT ALWFAEHASA DGIVHDTVCV
     TGTKGKSTTT ALVAHLLRAA GHRTGLVGNI GLPLLEVLDP QPAPEYWAVE LSSYQTGEVA
     RSGARPQVAV VLNLFPEHLD WHGSEQRYIE DKLQLVTEAA PRIAVLNAAD PHLAALSLPD
     SKVIWFNQPQ GWHMRGDIVH RGEQAVFDTR NTPLPGRHNR GNLCAVLAAL EALGLDAVAL
     APAVQDFRPL PNRLQRIGAA EGLTYVNDSI STTPHASLAA LECFAGQRIA LLVGGHDRGL
     DWTDFMQHMA HDVPPVEIVT MGSNGPRIHA MLQPLADAGR FGLHAAGDLP EAMALARAAL
     GSEGGVILLS PGAPSFGAYR DYVARGRHFA ELAGFDPDSI SAIPGLGIA
//

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