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Lactobacillus salivarius UCC118 (lsal0)
Gene : murD
DDBJ      :murD         UDP-N-acetylmuramoylalanine--D-glutamate ligase
Swiss-Prot:MURD_LACS1   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;         EC=6.3.2.9;AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;AltName: Full=D-glutamic acid-adding enzyme;

Homologs  Archaea  1/68 : Bacteria  855/915 : Eukaryota  6/199 : Viruses  0/175   --->[See Alignment]
c.5.1c.59.1c.72.2
:458 amino acids
:SECSTR
:PSIPRED
:DISOPRED
:BLT:PDB   7->444 2vtdA PDBj 2e-30 29.3 %
:RPS:PDB   2->39 2czgB PDBj 6e-05 31.6 %
:RPS:PDB   20->433 2am1A PDBj 2e-50 14.6 %
:RPS:SCOP  10->99 1gqqA1  c.5.1.1 * 4e-15 24.4 %
:RPS:SCOP  142->309 1j6uA3  c.72.2.1 * 7e-30 24.7 %
:RPS:SCOP  311->448 1e0dA2  c.59.1.1 * 1e-38 35.8 %
:HMM:SCOP  5->100 2uagA1 c.5.1.1 * 5e-22 44.4 %
:HMM:SCOP  101->309 2uagA3 c.72.2.1 * 3.5e-55 39.8 %
:HMM:SCOP  311->452 2uagA2 c.59.1.1 * 2.8e-41 46.4 %
:RPS:PFM   11->59 PF01262 * AlaDh_PNT_C 7e-05 50.0 %
:RPS:PFM   148->290 PF08245 * Mur_ligase_M 1e-11 37.7 %
:HMM:PFM   116->292 PF08245 * Mur_ligase_M 9.7e-51 47.3 165/188  
:HMM:PFM   312->380 PF02875 * Mur_ligase_C 3.1e-10 25.0 68/91  
:HMM:PFM   2->60 PF01262 * AlaDh_PNT_C 2.6e-10 39.7 58/168  
:BLT:SWISS 1->448 MURD_LACS1 0.0 100.0 %
:PROS 114->138|PS01011|FOLYLPOLYGLU_SYNT_1
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID ABD99859.1 GT:GENE murD GT:PRODUCT UDP-N-acetylmuramoylalanine--D-glutamate ligase GT:DATABASE GIB00337CH01 GT:ORG lsal0 GB:ACCESSION GIB00337CH01 GB:LOCATION complement(1075412..1076788) GB:FROM 1075412 GB:TO 1076788 GB:DIRECTION - GB:GENE murD GB:PRODUCT UDP-N-acetylmuramoylalanine--D-glutamate ligase GB:NOTE COG0771 [M] UDP-N-acetylmuramoylalanine-D-glutamate ligase GB:PROTEIN_ID ABD99859.1 GB:DB_XREF GI:90821220 GB:GENE:GENE murD LENGTH 458 SQ:AASEQ MKMIEKYRGKKVLVLGLGKSGVNAAKLLKKLGAEVTVNDKNTPSDLTQVNELKNEGIEVITGSHPLELLENIDLMVKNPGIPYTNVLVSGAKDKGIKIITEPELAFEISDARFVGVTGTNGKTTTTTMISLMLNQGQTEGKAYVAGNIGVPASQVAQEATSKDTIVTELSSFQLLGITEYHPKVAVLTNIYEAHIDYHGTRENYVNAKMRIVMNQTEDDYFVVNWDNEEWQELSQRSKAKIVPFSRLGKSKDGAYVAGGYLFYKEDKIMPVDNIKVPGTHNVENALAAIAVAKIFGKSNEDIKEVLTTFSGVRHRTQYVTTLNGRKFYNDSKATNMEATEKALAGFNNPVVLLAGGLDRGFTFEKLEPSLKNKVHAMIVFGETADLMAKAGKEAGVEKIIKTKDAVSAVPEAYKVSNEGDVILLSPACASWDQWPTFEVRGDKFIEAVEKLTEELEEK GT:EXON 1|1-458:0| SW:ID MURD_LACS1 SW:DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase; EC=6.3.2.9;AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;AltName: Full=D-glutamic acid-adding enzyme; SW:GN Name=murD; OrderedLocusNames=LSL_1051; SW:KW ATP-binding; Cell cycle; Cell division; Cell shape;Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;Ligase; Nucleotide-binding; Peptidoglycan synthesis. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->448|MURD_LACS1|0.0|100.0|448/458| GO:SWS:NREP 9 GO:SWS GO:0005524|"GO:ATP binding"|ATP-binding| GO:SWS GO:0007049|"GO:cell cycle"|Cell cycle| GO:SWS GO:0051301|"GO:cell division"|Cell division| GO:SWS GO:0008360|"GO:regulation of cell shape"|Cell shape| GO:SWS GO:0007047|"GO:cellular cell wall organization"|Cell wall biogenesis/degradation| GO:SWS GO:0005737|"GO:cytoplasm"|Cytoplasm| GO:SWS GO:0016874|"GO:ligase activity"|Ligase| GO:SWS GO:0000166|"GO:nucleotide binding"|Nucleotide-binding| GO:SWS GO:0009252|"GO:peptidoglycan biosynthetic process"|Peptidoglycan synthesis| PROS 114->138|PS01011|FOLYLPOLYGLU_SYNT_1|PDOC00773| SEG 115->127|gvtgtngkttttt| SEG 449->457|eklteelee| BL:PDB:NREP 1 BL:PDB:REP 7->444|2vtdA|2e-30|29.3|416/433| RP:PDB:NREP 2 RP:PDB:REP 2->39|2czgB|6e-05|31.6|38/403| RP:PDB:REP 20->433|2am1A|2e-50|14.6|391/442| RP:PFM:NREP 2 RP:PFM:REP 11->59|PF01262|7e-05|50.0|48/164|AlaDh_PNT_C| RP:PFM:REP 148->290|PF08245|1e-11|37.7|138/187|Mur_ligase_M| HM:PFM:NREP 3 HM:PFM:REP 116->292|PF08245|9.7e-51|47.3|165/188|Mur_ligase_M| HM:PFM:REP 312->380|PF02875|3.1e-10|25.0|68/91|Mur_ligase_C| HM:PFM:REP 2->60|PF01262|2.6e-10|39.7|58/168|AlaDh_PNT_C| GO:PFM:NREP 4 GO:PFM GO:0016491|"GO:oxidoreductase activity"|PF01262|IPR007698| GO:PFM GO:0055114|"GO:oxidation reduction"|PF01262|IPR007698| GO:PFM GO:0005524|"GO:ATP binding"|PF08245|IPR013221| GO:PFM GO:0009058|"GO:biosynthetic process"|PF08245|IPR013221| RP:SCP:NREP 3 RP:SCP:REP 10->99|1gqqA1|4e-15|24.4|86/89|c.5.1.1| RP:SCP:REP 142->309|1j6uA3|7e-30|24.7|162/207|c.72.2.1| RP:SCP:REP 311->448|1e0dA2|1e-38|35.8|134/140|c.59.1.1| HM:SCP:REP 5->100|2uagA1|5e-22|44.4|90/93|c.5.1.1|1/1|MurCD N-terminal domain| HM:SCP:REP 101->309|2uagA3|3.5e-55|39.8|201/204|c.72.2.1|1/1|MurD-like peptide ligases, catalytic domain| HM:SCP:REP 311->452|2uagA2|2.8e-41|46.4|138/140|c.59.1.1|1/1|MurD-like peptide ligases, peptide-binding domain| OP:NHOMO 1054 OP:NHOMOORG 862 OP:PATTERN ----------------------------------1--------------------------------- 1111121111111-11111-111112111111111111111111-1111111111111111111111111111111112112221121111211112--112121212111111111111111111111111111111111---111111111111111111111111111112111111111-----2312212222212312211122222112222224111222222421111111111111112111122222222222112222122211111111221112211111111111222222222222211111111112343222222223232211322221323112121122222321443212111-111211221111111111111122222222222-111111-1221222211212221111111111111121111111111111211-111--------1111111111111111111-21111111111111111111111111111111111111111111111-111111221121111111111121111121211111111111112111111111112211111111111-111111111111111111111111111111111111111111111111-1111111-11111111111111111111-111111111111111111111111111111111111111111111111111111111111111111112111111111111111111111111111112222221111111111111211112111111111111111111111111111111-1-1111111111112111111111111111---------------------------1111111111111 -----------------------------------------------------------------------------------------------------------------------------------------------------------------------------11---1------2-----2--1---- ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 448 STR:RPRED 97.8 SQ:SECSTR cccTTccTTccEEEEcccHcHHHHHHHHTcccccTTccccccccTTGGTTcGccTTcccccEEccGGGccTTcEEccccccccGGGGHHHHHHHTccEEEEccHHHHHHccEEEEEEcccccccHHHHHHHHTTTccEccEEccTTcccTTHHHHHHHTcTTcEEEEEccccTTHHHHHHcccEEEEccccccccTTcccHHHHHHHHGGGTccGTcTTcEEEEEccGGGGGGcccccEEEEEcTTccccEEEEEEccccEEEEETTcccEEEEccccHHHHHHHHHHHHHHHHTTccHHHHHHHGGGcccccccccEEccTTTcEEEEEcccccHHHHHTcccccccEEEEEEEcccccTTHHHGGGccTTTccEEEEEEcTTHHHHHHHHHccTTcEEEEEcccHHHHHHHHHccTTEEEEEEccccHHHHcccHHHHHHHHHHHH########## DISOP:02AL 1-4,453-459| PSIPRED ccccHHccccEEEEEcccHHHHHHHHHHHHcccEEEEEEcccccccHHHHHHHHcccEEEEccccHHccccccEEEEccccccccHHHHHHHHccccEEEHHHHHHHHccccEEEEEccccccHHHHHHHHHHHHccccccEEEcccccHHHHHHHcccccccEEEEEccccccccEEEEccEEEEEccccHHHHHHcccHHHHHHHHHHHHHccccccEEEEccccHHHHHHHHHccccEEEEEccccccccEEEEccEEEEEcccEEEEcccccccHHHHHHHHHHHHHHHHccccHHHHHHHHHHcccccccEEEEEccccEEEEEccccccHHHHHHHHHHccccEEEEEcccccccHHHHHHHHHHHcccEEEEEcccHHHHHHHHHHcccccEEEEccHHHHHHHHHHHcccccEEEEEccccHHHHHHHHHHHHHHHHHHHHHHHHHHHcc //