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Database: UniProt
Entry: A0A139SUW7_9GAMM
LinkDB: A0A139SUW7_9GAMM
Original site: A0A139SUW7_9GAMM 
ID   A0A139SUW7_9GAMM        Unreviewed;       444 AA.
AC   A0A139SUW7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:KXU38408.1};
GN   ORFNames=AXE65_01450 {ECO:0000313|EMBL:KXU38408.1};
OS   Ventosimonas gracilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ventosimonadaceae; Ventosimonas.
OX   NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU38408.1, ECO:0000313|Proteomes:UP000072660};
RN   [1] {ECO:0000313|EMBL:KXU38408.1, ECO:0000313|Proteomes:UP000072660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV58 {ECO:0000313|EMBL:KXU38408.1,
RC   ECO:0000313|Proteomes:UP000072660};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU38408.1}.
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DR   EMBL; LSZO01000135; KXU38408.1; -; Genomic_DNA.
DR   RefSeq; WP_068389535.1; NZ_LSZO01000135.1.
DR   AlphaFoldDB; A0A139SUW7; -.
DR   OrthoDB; 9809796at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000072660; 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   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:UP000072660}.
FT   DOMAIN          110..281
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          303..375
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         112..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   444 AA;  47469 MW;  E71F5F76536E8ED9 CRC64;
     MEHSRAIVLG LGKSGLSLVR ALRLRGCTVI GCDSRQNPPE LAALKREFPE VEVRLGAWHA
     DFLQSVDKVY VSPGISLKET ALQEAARRGV RFSGDMDLFS ELSKAPVVAI TGSNGKSTVT
     TLVGEMAKKA GKRVAVGGNL GTPALNLLAD DVELYVLELS SFQLETCREL SAEVACCLNL
     SEDHMDRYAD LDEYRAAKLR IFNGVNYQVV ATDCPDLKSA EPRPTFTFGE YQQGGDPKHF
     GLLFSRGVYH LSHGDSLLLP VSQLKIRGTH NQLNALAALA IGYAAGFPMQ AMLDALREFA
     GLPHRCQWLR ELHGVAWYND SKATNVGAAC AAINGLGADI DGKLVLIAGG DGKGADFSPL
     AEPVAQHCRA VLLIGRDADK LAAALPNTVV QQRVGGLEQA VKLAAQLAQT GDAVLLSPAC
     ASLDMFDNFE QRGDLFAKAV EALS
//
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