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Database: UniProt
Entry: Q07WI3_SHEFN
LinkDB: Q07WI3_SHEFN
Original site: Q07WI3_SHEFN 
ID   Q07WI3_SHEFN            Unreviewed;       440 AA.
AC   Q07WI3;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
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=Sfri_3806 {ECO:0000313|EMBL:ABI73631.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI73631.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI73631.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI73631.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00639,
CC         ECO:0000256|RuleBase:RU003664};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639}.
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DR   EMBL; CP000447; ABI73631.1; -; Genomic_DNA.
DR   RefSeq; WP_011639216.1; NC_008345.1.
DR   AlphaFoldDB; Q07WI3; -.
DR   STRING; 318167.Sfri_3806; -.
DR   KEGG; sfr:Sfri_3806; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_1_0_6; -.
DR   OMA; ACASYDQ; -.
DR   OrthoDB; 9809796at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000684; Chromosome.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   NCBIfam; TIGR01087; murD; 1.
DR   PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF21799; MurD-like_N; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684}.
FT   DOMAIN          114..280
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          301..363
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         116..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   440 AA;  46956 MW;  3B53D419254BBC95 CRC64;
     MQTQYTHIVL GLGATGLSVV RFLATKGIKP LVMDSRRHPP GADTLAQEFA DIELLAGGFD
     CRYLVQASQI IISPGVPIDT PEVRAALDMG IEVIGDVELF AREIADKKPC VVGITGSNGK
     STVTTLVYEM LLAAGKSVAI GGNIGTPALD LLPQNADFYV LELSSFQLET THSLNCIAAT
     CLNVSEDHMD RYSDLNTYRE AKLRLYPQSR FVMYNRDDEL TYPLEPMNQN NFGLGVPEGD
     AWGLSDGKIF HGDSEIINLI DVTLIGSHNH ANLLAAMALA DACGVGKEAM IEVAKSFVGL
     SHRCELIAVK QGVSYINDSK ATNVGATVAA LEGLNSHLGD LYLIAGGDGK GSDFRPLTEP
     LSNITQLITL GRDGRKIAKL KAGTIEVATM AEAVAKAAEL ASSGDIVLLS PACASLDMYK
     NFMARGDDFR QCVESLADGE
//
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