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Database: UniProt
Entry: I4VVZ4_9GAMM
LinkDB: I4VVZ4_9GAMM
Original site: I4VVZ4_9GAMM 
ID   I4VVZ4_9GAMM            Unreviewed;       457 AA.
AC   I4VVZ4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_02208};
DE            EC=6.3.2.53 {ECO:0000256|HAMAP-Rule:MF_02208};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_02208};
DE            Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000256|HAMAP-Rule:MF_02208};
GN   Name=murD {ECO:0000313|EMBL:EIL91385.1};
GN   Synonyms=murD2 {ECO:0000256|HAMAP-Rule:MF_02208};
GN   ORFNames=UU9_04452 {ECO:0000313|EMBL:EIL91385.1};
OS   Rhodanobacter fulvus Jip2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL91385.1, ECO:0000313|Proteomes:UP000004210};
RN   [1] {ECO:0000313|EMBL:EIL91385.1, ECO:0000313|Proteomes:UP000004210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC       {ECO:0000256|HAMAP-Rule:MF_02208}.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {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|RuleBase:RU003664};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC         glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC         EC=6.3.2.53; Evidence={ECO:0000256|HAMAP-Rule:MF_02208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_02208,
CC       ECO:0000256|RuleBase:RU003664}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_02208, ECO:0000256|RuleBase:RU003664}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02208}.
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:EIL91385.1}.
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DR   EMBL; AJXU01000021; EIL91385.1; -; Genomic_DNA.
DR   RefSeq; WP_007080531.1; NZ_AJXU01000021.1.
DR   AlphaFoldDB; I4VVZ4; -.
DR   STRING; 1163408.UU9_04452; -.
DR   PATRIC; fig|1163408.3.peg.916; -.
DR   eggNOG; COG0771; Bacteria.
DR   OrthoDB; 9809796at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000004210; 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-EC.
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   HAMAP; MF_02208; MurD2_subfam; 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; IPR043687; MurD2.
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_02208};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02208,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02208,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02208,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02208,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02208};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02208};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02208};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02208,
KW   ECO:0000256|RuleBase:RU003664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004210}.
FT   DOMAIN          115..276
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          298..373
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02208"
SQ   SEQUENCE   457 AA;  48586 MW;  7EEE2EEF42FDB4EB CRC64;
     MRIADLGGRR VAIWGFGREG RAALRALRQR CPDQHFTVFC SVAEVEAVHA FDAALEVIAG
     EPDAATLARF DIVVKSPGIS AYKPALLAAQ AQGTRFTSGT ALWFGEHPAA RVIAVTGTKG
     KSTTSALIAH LARALGVRTA LAGNIGLPLL ELLEQHADLW VIELSSFQTG EAGPLELGVI
     TSLYEEHLDW HGSREQYVID KLRLADVSRH WLVNALQPAL LQRTRQHPHR LLFGGPEGWH
     VAGDFICRGT QQVFPIAQLA APGLHNALNA CAALAALEAL GMDARAAAPA LASFRPLPHR
     LQPLGAHDGW HWVNDSISTT PLATLAALES LHGRTVTVLV GGHDRGLDWT PFVDAMRQAP
     AHAIICMGSN GARIESALRV ASAACPILLV GDLASAVEAA KMHTPAHGVI LLSPGAPSFD
     QFKDYAERGR RFSALAGFDA ANIASIDGLG IEGSPRD
//
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