ID   CHED1_ALBFT             Reviewed;         234 AA.
AC   Q221I2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Probable chemoreceptor glutamine deamidase CheD 1 {ECO:0000255|HAMAP-Rule:MF_01440};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_01440};
GN   Name=cheD1 {ECO:0000255|HAMAP-Rule:MF_01440}; OrderedLocusNames=Rfer_0570;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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: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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000267; ABD68321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q221I2; -.
DR   SMR; Q221I2; -.
DR   STRING; 338969.Rfer_0570; -.
DR   EnsemblBacteria; ABD68321; ABD68321; Rfer_0570.
DR   KEGG; rfr:Rfer_0570; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_0_4; -.
DR   OMA; VGMADLN; -.
DR   Proteomes; UP000008332; Chromosome.
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; Reference proteome.
FT   CHAIN           1..234
FT                   /note="Probable chemoreceptor glutamine deamidase CheD 1"
FT                   /id="PRO_0000251060"
SQ   SEQUENCE   234 AA;  25245 MW;  433639F7C7529B25 CRC64;
     MNMFASGTAA LPLRASGVVV APTVLAGGAL SRVDQLKAQI RNPGEASFFY RDHHFQYDAV
     KVLPGEYFVS AEDLVIMTVL GSCISACIWD GRVRAGGMNH FMLPDGDSVD GFGRYGSYAM
     ELLINELLKK GARRESMQAK VFGGAAVMAG FTTMNVGERN TKFVLDYLAT ERIPVVSQDV
     LDIHPRKVCF FPVTGKVLVK RLAHSHPETL AVEERKGNAA TVAKATSGGS VDLF