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Database: UniProt
Entry: A0A1Z5IGY3_9LACO
LinkDB: A0A1Z5IGY3_9LACO
Original site: A0A1Z5IGY3_9LACO 
ID   A0A1Z5IGY3_9LACO        Unreviewed;       234 AA.
AC   A0A1Z5IGY3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=IWT126_01052 {ECO:0000313|EMBL:GAX01027.1};
OS   Secundilactobacillus silagei JCM 19001.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1302250 {ECO:0000313|EMBL:GAX01027.1, ECO:0000313|Proteomes:UP000198402};
RN   [1] {ECO:0000313|EMBL:GAX01027.1, ECO:0000313|Proteomes:UP000198402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT126 {ECO:0000313|EMBL:GAX01027.1,
RC   ECO:0000313|Proteomes:UP000198402};
RA   Tohno M., Tanizawa Y., Arita M.;
RT   "Draft genome sequences of new species of the genus Lactobacillus isolated
RT   from orchardgrass silage.";
RL   Submitted (NOV-2015) 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}.
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:GAX01027.1}.
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DR   EMBL; BCMG01000004; GAX01027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5IGY3; -.
DR   STRING; 1302250.GCA_001313225_00619; -.
DR   OrthoDB; 9782045at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000198402; 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          6..201
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        95
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ   SEQUENCE   234 AA;  25685 MW;  DCED8A28C76EEAED CRC64;
     MTYELNVAHL YGDLMNTYGD VGNILALNYY AKQMDVKLNV KVVSLDQDFK AADYDLAFFG
     GGQDFEQVIV SKDIQTKKKE LTAFIEDGGP VLAICGGFQL LGHYYVDAKG DKIPGIGALD
     HYTLSQDNHR FIGDIVIKNA DNGETYHGFE NHQGRTFLGK AESPLGNVVQ GKGNNGEDGT
     EGAIYKNVYC SYFHGPILTR NGNLAKRLLV AALKRSYPDA DFSEQEALPV PATF
//
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