ID E1QZC0_OLSUV Unreviewed; 253 AA.
AC E1QZC0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=Olsu_0619 {ECO:0000313|EMBL:ADK67734.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67734.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK67734.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
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; CP002106; ADK67734.1; -; Genomic_DNA.
DR RefSeq; WP_013251486.1; NZ_JQCO01000001.1.
DR AlphaFoldDB; E1QZC0; -.
DR STRING; 633147.Olsu_0619; -.
DR GeneID; 78512040; -.
DR KEGG; ols:Olsu_0619; -.
DR PATRIC; fig|633147.7.peg.933; -.
DR eggNOG; COG3442; Bacteria.
DR HOGENOM; CLU_064047_0_0_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000333; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000000333};
KW Transferase {ECO:0000313|EMBL:ADK67734.1}.
FT DOMAIN 12..205
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ SEQUENCE 253 AA; 27556 MW; 086582F2025D4DDF CRC64;
MADVASVPRV LRVAHLYPEL LNLYGDSGNI LVLRSRMAWR GIGCEVREVH VGERPSFSDV
DIAFIGGGSD REERIVCDKL LAERAELCSF VEDGGVLAAV CGGYQLLGDS YLMGDERVGG
LGLVDLYTDR GTPRLIGNIA VESRISPQPI VGYENHGGRT HLGPGVEPLG RVLYGHGNDG
QTGWEGCLYK NVMGTYVHGP LLPKNPGVAD HLIRRALERK YGASELDPLD DEEELAANKV
MFDRLMAGEV KER
//
