GenomeNet

Database: UniProt
Entry: A0A1M4S3S1_9ACTO
LinkDB: A0A1M4S3S1_9ACTO
Original site: A0A1M4S3S1_9ACTO 
ID   A0A1M4S3S1_9ACTO        Unreviewed;       254 AA.
AC   A0A1M4S3S1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=ACGLYG10_3074 {ECO:0000313|EMBL:SHE26819.1};
OS   Actinomyces glycerinitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1892869 {ECO:0000313|EMBL:SHE26819.1, ECO:0000313|Proteomes:UP000184291};
RN   [1] {ECO:0000313|Proteomes:UP000184291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Strepis N.;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQTT01000016; SHE26819.1; -; Genomic_DNA.
DR   RefSeq; WP_073333906.1; NZ_FQTT01000016.1.
DR   AlphaFoldDB; A0A1M4S3S1; -.
DR   STRING; 1892869.ACGLYG10_3074; -.
DR   OrthoDB; 9782045at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000184291; 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   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:UP000184291}.
FT   DOMAIN          22..213
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ   SEQUENCE   254 AA;  27392 MW;  C1C019306F7FC234 CRC64;
     MSTDPTVYNH TGSGPARGRI RVLQLYPRDM NIYGDWGNLL TLARRGQWHG YDVELHSYNP
     GDEMPQEVDL VLGGGGQDSG QERIKDDLVQ IGPRLRQWAA DGVPMLVICG LYQLFGHRFV
     TGERSEIPGI GLLDAETVAG SGRLIGNIVL DSPEFGRVVG YENHSGLTTL GPGAEPLGTV
     RSGAGNNGKD GAEGARFKHV IGTYLHGPIL PKNPAVADWL LQRAVELRSG AWDPLPIDDA
     DARRASNVAA SRPR
//
DBGET integrated database retrieval system