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Database: UniProt
Entry: A0A1I2QC89_9SPHN
LinkDB: A0A1I2QC89_9SPHN
Original site: A0A1I2QC89_9SPHN 
ID   A0A1I2QC89_9SPHN        Unreviewed;       183 AA.
AC   A0A1I2QC89;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=SAMN05518801_11269 {ECO:0000313|EMBL:SFG25550.1};
OS   Novosphingobium sp. CF614.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1884364 {ECO:0000313|EMBL:SFG25550.1, ECO:0000313|Proteomes:UP000199304};
RN   [1] {ECO:0000313|EMBL:SFG25550.1, ECO:0000313|Proteomes:UP000199304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF614 {ECO:0000313|EMBL:SFG25550.1,
RC   ECO:0000313|Proteomes:UP000199304};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOOR01000012; SFG25550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2QC89; -.
DR   STRING; 1884364.SAMN05518801_11269; -.
DR   OrthoDB; 9807202at2; -.
DR   Proteomes; UP000199304; 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:UP000199304}.
SQ   SEQUENCE   183 AA;  20163 MW;  A6FB859779E1D4DB CRC64;
     MALDLNLDNV TRLTVLQGQF KISAGPKVEL GTVLGSCVAT CLFDPVVELG GMNHFLLPEP
     PASHNRGEVD VHYGVYLMEM LINEMLSYGA RKERLRAHLY GGANIRAGMQ QIGTANAEFA
     RSFLVRERIE LVREDLGGTN ARRVEFRPAS GKVRCRTVAS SDAPEAKPQP VFRPVPRGEV
     ELF
//
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