(data stored in SCRATCH zone)

SWISSPROT: A8FQ98_SHESH

ID   A8FQ98_SHESH            Unreviewed;       443 AA.
AC   A8FQ98;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 76.
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=Ssed_0408 {ECO:0000313|EMBL:ABV35021.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35021.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35021.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35021.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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}.
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DR   EMBL; CP000821; ABV35021.1; -; Genomic_DNA.
DR   RefSeq; WP_012140758.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ98; -.
DR   STRING; 425104.Ssed_0408; -.
DR   EnsemblBacteria; ABV35021; ABV35021; Ssed_0408.
DR   KEGG; sse:Ssed_0408; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049427; -.
DR   KO; K01925; -.
DR   OMA; VDKGNDY; -.
DR   OrthoDB; POG091H002Z; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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; IPR004101; Mur_ligase_C.
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; A8FQ98.
DR   SWISS-2DPAGE; A8FQ98.
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:UP000002015};
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:ABV35021.1};
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}.
FT   DOMAIN      114    280       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      301    372       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     116    122       ATP. {ECO:0000256|HAMAP-Rule:MF_00639}.
SQ   SEQUENCE   443 AA;  47222 MW;  3BDB65BAF076F357 CRC64;
     MVNHKSHLIL GLGATGLSVV RYLHGLGITP LVMDSRQQPP GADKLAAEFP DVELISGGFD
     CRYLVQATQI IVSPGIAIDT PEIRAAIDMD IEVIGDVELF ARAVKERDAC VIGITGSNGK
     STVTTLVAEM AKAAGINYAV GGNIGIPVLD LLQSDIELYV LELSSFQLET THSLNCISAT
     CLNISEDHMD RYSDIEAYRQ AKLRLYSQTR FALFNREDEL TKPKDPMNQN SFGLSLPDND
     EWGVCEGKIV HGSVEVISLQ DVALVGSHNH ANLIAAMALA YQAGIEKAAM VEVASSFTGL
     EHRFEMVVNR NGVAYINDSK ATNVGATVAA IEGISEHLGD IILIAGGDGK GADFKPLVPV
     LKAVSHLITL GKDGDKIAAL SDSSIRVDSM ADAVNKAAQL AIAGDIVLLS PACASLDMYK
     NFMERGDDFR RLAEGLSAEA LNA
//

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