ID H5TDL2_9ALTE Unreviewed; 491 AA.
AC H5TDL2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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:GAB56389.1};
GN ORFNames=GPUN_2274 {ECO:0000313|EMBL:GAB56389.1};
OS Glaciecola punicea ACAM 611.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB56389.1, ECO:0000313|Proteomes:UP000053586};
RN [1] {ECO:0000313|EMBL:GAB56389.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56389.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=22628500; DOI=10.1128/JB.00463-12;
RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT punicea ACAM 611T.";
RL J. Bacteriol. 194:3267-3267(2012).
RN [2] {ECO:0000313|EMBL:GAB56389.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56389.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAB56389.1}.
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DR EMBL; BAET01000028; GAB56389.1; -; Genomic_DNA.
DR RefSeq; WP_006006491.1; NZ_BAET01000028.1.
DR AlphaFoldDB; H5TDL2; -.
DR STRING; 56804.BAE46_05220; -.
DR eggNOG; COG0771; Bacteria.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053586; 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:UP000053586}.
FT DOMAIN 132..274
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 344..417
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 134..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 491 AA; 52782 MW; 11E58FCF7FAF52FA CRC64;
MRPLANAYSY ENQSVAIIGY GVTGKACVAF LLNKGAKVSV FDDSFNTSNK QSLANTENLT
FCEVHEALDL REFDQVVVSP GVNLRKAFIQ NYIAHKGHAS AVIGDIELFA RQLNEINSGL
VPGENPIKVV AVTGSNGKST VVDMLTKVLL KQGVNVALGG NFGTAALALI APNFILAGNN
GHSEQNTSAP RIDIIVLELS SFQLESTFSL CPDIGCILNI SSDHLDRHGS MAAYTLAKQQ
IYANAATVVF NRDDSATSPS SLENAISVGY NQFDGGQLGD STKHFYQTSK GIYCGQHFLF
DASQVMGISQ FQLVNMQVVF ACCQILKVNL VLAAQSLGEY KGLPHRFETV YHSKTSIWIN
DSKATNPGAC LAALESLAKQ VSHIILIAGG DAKGADIQML AHAMSTHVDR LILIGKDADL
FTQFGTPFTR ANSIEDAVEK AKAYAGELAR NHDNPYIGVM LSPACASIDM FNNYQHRGQL
FCQAVTAQVT A
//
