ID D6ZCA5_SEGRD Unreviewed; 248 AA.
AC D6ZCA5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=Srot_2640 {ECO:0000313|EMBL:ADG99074.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG99074.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG99074.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(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; CP001958; ADG99074.1; -; Genomic_DNA.
DR RefSeq; WP_013139523.1; NC_014168.1.
DR AlphaFoldDB; D6ZCA5; -.
DR STRING; 640132.Srot_2640; -.
DR KEGG; srt:Srot_2640; -.
DR eggNOG; COG3442; Bacteria.
DR HOGENOM; CLU_064047_2_0_11; -.
DR OrthoDB; 9782045at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002247; 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:UP000002247};
KW Transferase {ECO:0000313|EMBL:ADG99074.1}.
FT DOMAIN 12..207
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT ACT_SITE 200
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
SQ SEQUENCE 248 AA; 25662 MW; F83A13F5E26C4022 CRC64;
MSPAEPRQEV LRIGLVLPDV MGTYGDSGNA TVLEQRATLR GIPAEVVTIT LDDPVPDSLD
IYTIGGAEDA AQRLATEHLL AHQGLQRAAA KGAPVLAICA ALQVLGEWYE LAEGTKIAGV
GLLDVTTRGR SGARSIGEVV LEPRLAGLSE PITGFENHGG ASSLGPACQP LGAVKAGDGN
AAGEPVEGAV QGSVVSTYLH GPVLARNPQL ADLLLARALG VPMQELAPLD LPSVRLLREE
RFAAPRRG
//
