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Database: UniProt
Entry: D6Z3Q2_DESAT
LinkDB: D6Z3Q2_DESAT
Original site: D6Z3Q2_DESAT 
ID   D6Z3Q2_DESAT            Unreviewed;       497 AA.
AC   D6Z3Q2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=DaAHT2_1482 {ECO:0000313|EMBL:ADH86177.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH86177.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) 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; CP001940; ADH86177.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6Z3Q2; -.
DR   STRING; 589865.DaAHT2_1482; -.
DR   KEGG; dak:DaAHT2_1482; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_0_0_7; -.
DR   InParanoid; D6Z3Q2; -.
DR   OMA; ACASYDQ; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001508; 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:UP000001508}.
FT   DOMAIN          127..317
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          339..406
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         129..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   497 AA;  51563 MW;  195BDC448EAC29BA CRC64;
     MLMLMAGDDM TFAGSLTGKH VLVVGLGKSG CAAARFLVKQ GVRISVSEGG RAVAPASRMV
     QWLQERGVYC ELGGHSPQLF AGVDVILLSP GIPLDIPALD AARAAGVPII GELALAPEYL
     RTPVIAVTGT NGKSTVTTLV GELLRAAGRN VFVGGNLGTP LCEYLAGPQE ADWAVLEVSS
     FQLDSAGKFS PDIAVLLNIS PDHLDRYPDY AAYAASKWRI VANQGREQWA VINRDDPEIL
     RLLAAGPPAS RVFGFGGRGM AGPLAANQSR EAAPGPPVDG LRLCLTQEDE HCEEYPLPAN
     ELAVEPNRQN ALAAVLAARL AGCPPAAVGP ALAAFQALPH RLALVATVAG VRYYDDSKAT
     NIGAVISALQ GLPGPVVLIA GGLDKGGDYR LLLPAIKEKV RAVVLIGSAR EKMRAALAPA
     VPVTEAADLP SAVRIATQLA AAGEAVLLSP ACASFDMFAG YAQRGEVFRR AVRELAEDNA
     LGGGAVGHCP AMEAMFA
//
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