ID   CHED_MOOTA              Reviewed;         167 AA.
AC   Q2RKC1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000255|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   Name=cheD {ECO:0000255|HAMAP-Rule:MF_01440}; OrderedLocusNames=Moth_0800;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
CC   -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC       methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC       in chemotaxis. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01440};
CC   -!- SIMILARITY: Belongs to the CheD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01440}.
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DR   EMBL; CP000232; ABC19118.1; -; Genomic_DNA.
DR   RefSeq; WP_011392321.1; NC_007644.1.
DR   RefSeq; YP_429661.1; NC_007644.1.
DR   AlphaFoldDB; Q2RKC1; -.
DR   SMR; Q2RKC1; -.
DR   STRING; 264732.Moth_0800; -.
DR   EnsemblBacteria; ABC19118; ABC19118; Moth_0800.
DR   KEGG; mta:Moth_0800; -.
DR   PATRIC; fig|264732.11.peg.859; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_2_0_9; -.
DR   OMA; VGMADLN; -.
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; PTHR35147; 1.
DR   Pfam; PF03975; CheD; 1.
DR   SUPFAM; SSF64438; SSF64438; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Hydrolase.
FT   CHAIN           1..167
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000251045"
SQ   SEQUENCE   167 AA;  18004 MW;  3F6889BDFFE7E1D4 CRC64;
     MEAIIKPQEV KVGIAEWQVL RAPGRLITLG LGSCVGIALY DSLNRMGGLA HIMLPDSSQF
     QDRSNRAKFA DLAILDLVAA LIGRGARRGR LVAKIAGGAQ MFTSGDRHLS LLNIGQRNAA
     MVRQTLQELA IPLVAEDTGG NYGRTMIFDL ESGDVLIRTI GRPLKVI