ID A0A239VBM1_9MICO Unreviewed; 308 AA.
AC A0A239VBM1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMEA4475696_00738 {ECO:0000313|EMBL:SNV19565.1};
OS Dermatophilus congolensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Dermatophilus.
OX NCBI_TaxID=1863 {ECO:0000313|EMBL:SNV19565.1, ECO:0000313|Proteomes:UP000242637};
RN [1] {ECO:0000313|EMBL:SNV19565.1, ECO:0000313|Proteomes:UP000242637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13039 {ECO:0000313|EMBL:SNV19565.1,
RC ECO:0000313|Proteomes:UP000242637};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906453; SNV19565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239VBM1; -.
DR STRING; 1121387.GCA_000429885_01835; -.
DR KEGG; dco:SAMEA4475696_0738; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000242637; Chromosome 1.
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:UP000242637}.
FT DOMAIN 45..236
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT ACT_SITE 229
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ SEQUENCE 308 AA; 32683 MW; A691066C4C54836C CRC64;
MTISSTSVSE EMHGSGTLTA ADAPGALQSG SMADSYHGPV KGKLKIVHLY PREMSIYGDF
GNVRALQVRA QRHGYEVEVL AHHPGTVLRD DVDIIVGGGG QDSGQARVED DLAANGDMLR
QLAADKAPML VVCGMYQLLG RDFTTVAGKR LPGLGILDVT TTGAETRMVG PVVISGKFGE
MVGYENHSGR TLRGPGQAAL GTVLYGQGND GQDGTEGAVK DNVYGTYLHG PVLPSNPAFT
DELLRAAVER QDKGGFEPEA LDDTLADEAR HRQVERLLAG YDDGGSSVLP SVRDVARAAL
RRARAMRR
//
