ID S6FGS7_LACLL Unreviewed; 261 AA.
AC S6FGS7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD {ECO:0000256|HAMAP-Rule:MF_02213};
DE EC=6.3.5.13 {ECO:0000256|HAMAP-Rule:MF_02213};
DE AltName: Full=Lipid II isoglutaminyl synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_02213};
DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_02213};
GN Name=cobQ {ECO:0000313|EMBL:CDG04526.1};
GN Synonyms=gatD {ECO:0000256|HAMAP-Rule:MF_02213};
GN ORFNames=O9U_12875 {ECO:0000313|EMBL:CDG04526.1};
OS Lactococcus lactis subsp. lactis A12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1137134 {ECO:0000313|EMBL:CDG04526.1, ECO:0000313|Proteomes:UP000015361};
RN [1] {ECO:0000313|EMBL:CDG04526.1, ECO:0000313|Proteomes:UP000015361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A12 {ECO:0000313|EMBL:CDG04526.1,
RC ECO:0000313|Proteomes:UP000015361};
RX PubMed=23872564; DOI=10.1128/AEM.01560-13;
RA Passerini D., Coddeville M., Le Bourgeois P., Loubiere P., Ritzenthaler P.,
RA Fontagne-Faucher C., Daveran-Mingot M.L., Cocaign-Bousquet M.;
RT "The Carbohydrate Metabolism Signature of Lactococcus lactis Strain A12
RT Reveals Its Sourdough Ecosystem Origin.";
RL Appl. Environ. Microbiol. 79:5844-5852(2013).
CC -!- FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the
CC formation of alpha-D-isoglutamine in the cell wall lipid II stem
CC peptide. The GatD subunit catalyzes the hydrolysis of glutamine to
CC glutamate and ammonia. The resulting ammonia molecule is channeled to
CC the active site of MurT. {ECO:0000256|HAMAP-Rule:MF_02213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-
CC D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-
CC glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-
CC isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
CC diphosphate + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:57928,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:60033, ChEBI:CHEBI:62233, ChEBI:CHEBI:456216;
CC EC=6.3.5.13; Evidence={ECO:0000256|HAMAP-Rule:MF_02213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02213};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02213}.
CC -!- SUBUNIT: Forms a heterodimer with MurT. {ECO:0000256|HAMAP-
CC Rule:MF_02213}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. GatD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02213}.
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:CDG04526.1}.
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DR EMBL; CBLU010000011; CDG04526.1; -; Genomic_DNA.
DR RefSeq; WP_021722506.1; NZ_CBLU010000011.1.
DR AlphaFoldDB; S6FGS7; -.
DR GeneID; 69713117; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015361; Unassembled WGS sequence.
DR GO; GO:0140282; F:carbon-nitrogen ligase activity on lipid II; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_02213; Lipid_II_synth_GatD; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR043702; Lipid_II_synth_GatD.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR PANTHER; PTHR21343:SF9; LIPID II ISOGLUTAMINYL SYNTHASE (GLUTAMINE-HYDROLYZING) SUBUNIT GATD; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02213};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02213};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_02213,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02213};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02213};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02213}.
FT DOMAIN 18..214
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT ACT_SITE 207
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ SEQUENCE 261 AA; 29340 MW; 0DCF356684A95225 CRC64;
MAYISLKSNL ENPKYSLNVA HLYGDLMNTY GDNGNILMLK YVGEKLGAEM TFNIVSLGDT
FAKEDYDLVF WGGGQDYEQE IIADQSLLDL SAPLKDYIES EKPLLAICGG YQMLGQYYVN
SEGTKIQGTG ILGHYTENLR TDRFIGDIET HNEEFGETYY GFENHSGITY LSDDEKPLGT
VVYGGGNNPD DQTEGLIYKN TFGTYFHGPI LSRNARLAYR LVTTALYQKY GEEIQLPAFE
EILADEDKGQ QIGDLKRKVE K
//
