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Database: UniProt
Entry: A0A1N7NZE1_9RHOB
LinkDB: A0A1N7NZE1_9RHOB
Original site: A0A1N7NZE1_9RHOB 
ID   A0A1N7NZE1_9RHOB        Unreviewed;       467 AA.
AC   A0A1N7NZE1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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   ORFNames=SAMN05421759_11167 {ECO:0000313|EMBL:SIT03717.1};
OS   Roseivivax lentus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=633194 {ECO:0000313|EMBL:SIT03717.1, ECO:0000313|Proteomes:UP000186684};
RN   [1] {ECO:0000313|EMBL:SIT03717.1, ECO:0000313|Proteomes:UP000186684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29430 {ECO:0000313|EMBL:SIT03717.1,
RC   ECO:0000313|Proteomes:UP000186684};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTOQ01000011; SIT03717.1; -; Genomic_DNA.
DR   RefSeq; WP_076449389.1; NZ_FTOQ01000011.1.
DR   AlphaFoldDB; A0A1N7NZE1; -.
DR   STRING; 633194.SAMN05421759_11167; -.
DR   OrthoDB; 9809796at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000186684; Unassembled WGS sequence.
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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00639};
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|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00639}.
FT   DOMAIN          125..310
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          331..377
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         127..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   467 AA;  48819 MW;  7EC4427A01AA0E98 CRC64;
     MIPVDGVAGE KVGVLGLGRS GLSAARALRE GGAVPILWDD NPAARAAAEA EGFETRDLGA
     AGAMDDLTLL VTSPGIPHLY PEPNRVIAAA YAACVPVDND IGLFFRALSS GAWDDLETPP
     KVVAVTGSNG KSTTSALIHH ILSEAGREVQ LAGNIGRGVL DIDPPGEAGV IVLELSSYQT
     ELARALTPDI AVFTNLSPDH LDRHAGLGGY FAAKRRLFAE GGPDRAVIGV DEPEGRYLAN
     QLATARSDDR VIRVSVGQKL SGPGWIVQAR KGFLTEWRKG KQVGAIDLRE IPGLPGAHNH
     QNACAAYAAA RTLGLGPRQI EAALRTFKGL PHRSQIVAER DGVRFVNDSK ATNVDAALKA
     LLAFDRIRWV CGGLMKEGGL AALAPGLPHV AKAYVIGREA AQFALGLDGV EAEVCTDMGT
     AVARAAAEAE PGDVVLLAPA AASFDQYDNF EKRGEDFAAQ VAAFLGS
//
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