ID A0A1J0A6P4_9ENTE Unreviewed; 228 AA.
AC A0A1J0A6P4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=gatD {ECO:0000256|HAMAP-Rule:MF_02213};
GN ORFNames=BHY08_07000 {ECO:0000313|EMBL:APB31596.1};
OS Vagococcus teuberi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31596.1, ECO:0000313|Proteomes:UP000191200};
RN [1] {ECO:0000313|EMBL:APB31596.1, ECO:0000313|Proteomes:UP000191200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31596.1,
RC ECO:0000313|Proteomes:UP000191200};
RA Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA Stevens M.J., Meile L.;
RT "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT fene.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP017267; APB31596.1; -; Genomic_DNA.
DR RefSeq; WP_071457189.1; NZ_CP017267.1.
DR AlphaFoldDB; A0A1J0A6P4; -.
DR STRING; 519472.BHY08_07000; -.
DR KEGG; vte:BHY08_07000; -.
DR OrthoDB; 9782045at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000191200; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000191200}.
FT DOMAIN 9..202
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT ACT_SITE 195
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ SEQUENCE 228 AA; 25984 MW; A07B7C473A33ADBF CRC64;
MTNYHLTFCH LYGNLLNTYG DNGNLLLLNY YAKKLGITID TEIISVFEDF DETKYDFVFF
GGGQDYEQKI VSEDIQTKKD AITRYIENDG VMLAICGGFQ LLGEYYIGAH GEKIEGISAL
PHYTLSQDNN RFIGDIEIYN KEFDETYYGF ENHNGMTFLG EGEKPLGEVV KGYGNNGKDK
TEGVIYKNVI GSYFHGPLLA KNKQLALRLL NMAMKTKYEK TFKLKELN
//
