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Database: UniProt
Entry: K6W4V8_9MICO
LinkDB: K6W4V8_9MICO
Original site: K6W4V8_9MICO 
ID   K6W4V8_9MICO            Unreviewed;       264 AA.
AC   K6W4V8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=AUCHE_03_00740 {ECO:0000313|EMBL:GAB76857.1};
OS   Austwickia chelonae NBRC 105200.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Austwickia.
OX   NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB76857.1, ECO:0000313|Proteomes:UP000008495};
RN   [1] {ECO:0000313|EMBL:GAB76857.1, ECO:0000313|Proteomes:UP000008495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB76857.1,
RC   ECO:0000313|Proteomes:UP000008495};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL   Submitted (AUG-2012) 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:GAB76857.1}.
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DR   EMBL; BAGZ01000003; GAB76857.1; -; Genomic_DNA.
DR   RefSeq; WP_006501608.1; NZ_BAGZ01000003.1.
DR   AlphaFoldDB; K6W4V8; -.
DR   STRING; 100225.SAMN05421595_1991; -.
DR   eggNOG; COG3442; Bacteria.
DR   OrthoDB; 9782045at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008495; 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:UP000008495}.
FT   DOMAIN          22..211
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        108
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ   SEQUENCE   264 AA;  28672 MW;  F2CE77EE309F7049 CRC64;
     MSTQDVVVTH PEGESKGTVV LVHIYPKEMS IYGDLGNTRV LQRRLNWHGY SCRLHRHHPG
     QDFPEDAHIV LGGGGQDSGQ ARVESDLDRN GDVLKALADD GCPMLMICGM YQLFGNAFVT
     LEGRRLPGLG ILDVTTTGNT TRMISPVVLE TDYGKIVGYE NHSGATVLGP GQQAFGRVLH
     GYGNNPEDGT EGARTKRVFG TYLHGPILPA NPVFADALIA AAVERGLGRP FDSEDIDDTL
     AVQARERQIT RLLSGKEKRD RKGA
//
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