ID A0A0G3I7V2_LIBAF Unreviewed; 468 AA.
AC A0A0G3I7V2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639};
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=G293_05135 {ECO:0000313|EMBL:AKK20638.1};
OS Candidatus Liberibacter africanus PTSAPSY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1277257 {ECO:0000313|EMBL:AKK20638.1, ECO:0000313|Proteomes:UP000035503};
RN [1] {ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|Proteomes:UP000035503};
RA Lin H., Pietersen G., Sahota P., Lou B., Han S., Read D.A., Civerolo E.L.,
RA Gupta G.;
RT "Complete genome sequence of 'Candidatus Liberibacter africanus, bacterium
RT associated with citrus huanglongbing'.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK20638.1, ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|EMBL:AKK20638.1,
RC ECO:0000313|Proteomes:UP000035503};
RX PubMed=26184931;
RA Lin H., Pietersen G., Han C., Read D.A., Lou B., Gupta G., Civerolo E.L.;
RT "Complete Genome Sequence of 'Candidatus Liberibacter africanus,' a
RT Bacterium Associated with Citrus Huanglongbing.";
RL Genome Announc. 3:e00733-15(2015).
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}.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00639}.
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DR EMBL; CP004021; AKK20638.1; -; Genomic_DNA.
DR RefSeq; WP_047264588.1; NZ_CP004021.1.
DR AlphaFoldDB; A0A0G3I7V2; -.
DR STRING; 1277257.G293_05135; -.
DR KEGG; lau:G293_05135; -.
DR PATRIC; fig|1277257.4.peg.1119; -.
DR OrthoDB; 9809796at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000035503; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR036565; Mur-like_cat_sf.
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; PF07991; IlvN; 1.
DR Pfam; PF08245; Mur_ligase_M; 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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..468
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002555434"
FT DOMAIN 6..59
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|Pfam:PF07991"
FT DOMAIN 118..291
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT BINDING 120..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ SEQUENCE 468 AA; 52120 MW; 1298F3B409D5652D CRC64;
MKLRSFKNHS IAIFGLGSSG LSVANSLNNS GAHVIAWDDH PVAVKKAQDM GIKVVDFRTI
SWSNINYLVL SPGIALTGEN AHWCVTLANQ FNVEIIGDIE LFVRERRFSL QQSLFIAVTG
TNGKSSTVAL IAHILQNNGY DVQLGGNIGL PILNLEYFVP NRFYVIECSS YQIELAPTID
PSIGVLLNIS PDHLDRHHSL DNYVRIKEKI VKMSKHAIIC TQDDQCKKIA SDVNCCEHSI
SRISSKLMPL DSDLYIDEYS LKCSSTSKII FDFSREIKKH NIQNLAASAT VCMRLGLKND
DIKRALSSFD GLTHRLQTIA QLGDVIFIND SKATNLHSVV NAISNEKRAI YWIAGGVSKS
EDFSILFPLL SKIAKAYFIG DSSMLFSHHL GCKIHSTISN TLDQALKSAI RDAENTQLSS
VILFSPGCAS FDQYTDFRER GFSFMSLVSE IKDIEMFVDI EKERQSPW
//
