ID A0A0A0M725_9GAMM Unreviewed; 200 AA.
AC A0A0A0M725;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000256|HAMAP-Rule:MF_01440};
DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_01440};
GN Name=cheD {ECO:0000256|HAMAP-Rule:MF_01440};
GN ORFNames=N791_14330 {ECO:0000313|EMBL:KGO97989.1};
OS Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO97989.1, ECO:0000313|Proteomes:UP000030003};
RN [1] {ECO:0000313|EMBL:KGO97989.1, ECO:0000313|Proteomes:UP000030003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO97989.1,
RC ECO:0000313|Proteomes:UP000030003};
RA Wang Q., Wang G.;
RT "Genomic analysis of Lysobacter defluvii.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC in chemotaxis. {ECO:0000256|HAMAP-Rule:MF_01440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01440};
CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000256|HAMAP-
CC Rule:MF_01440}.
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:KGO97989.1}.
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DR EMBL; AVBH01000153; KGO97989.1; -; Genomic_DNA.
DR RefSeq; WP_027069395.1; NZ_AVBH01000153.1.
DR AlphaFoldDB; A0A0A0M725; -.
DR STRING; 1385515.GCA_000423325_00933; -.
DR eggNOG; COG1871; Bacteria.
DR OrthoDB; 9807202at2; -.
DR Proteomes; UP000030003; Unassembled WGS sequence.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16352; CheD; 1.
DR Gene3D; 3.30.1330.200; -; 1.
DR HAMAP; MF_01440; CheD; 1.
DR InterPro; IPR038592; CheD-like_sf.
DR InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR PANTHER; PTHR35147; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR PANTHER; PTHR35147:SF2; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR Pfam; PF03975; CheD; 1.
DR SUPFAM; SSF64438; CNF1/YfiH-like putative cysteine hydrolases; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW Rule:MF_01440};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01440};
KW Reference proteome {ECO:0000313|Proteomes:UP000030003}.
SQ SEQUENCE 200 AA; 21192 MW; 73AE098E04DA62D7 CRC64;
MAAAAPVTEA GSYWDAELST HAVRLLPADY RVSGEPLALV TLLGSCVAAC LYDPAVGVGG
MNHFLLPGGH AGSGEDPSAR YGVHAMELLV NALLKRGARR QRLQAKVFGG GNVLSGFHLD
PVGTRNARFV LQYLAAEGIP VVAQDLDGIQ ARKVCFFVQT GRTLVKRLPP TRGDDEIVRA
ERAYLGNLSR APVAGSVELF
//
