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Database: UniProt
Entry: N2IMS3_9PSED
LinkDB: N2IMS3_9PSED
Original site: N2IMS3_9PSED 
ID   N2IMS3_9PSED            Unreviewed;       173 AA.
AC   N2IMS3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=HMPREF1487_08691 {ECO:0000313|EMBL:ENA28702.1};
OS   Pseudomonas sp. HPB0071.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA28702.1, ECO:0000313|Proteomes:UP000017050};
RN   [1] {ECO:0000313|EMBL:ENA28702.1, ECO:0000313|Proteomes:UP000017050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPB0071 {ECO:0000313|EMBL:ENA28702.1,
RC   ECO:0000313|Proteomes:UP000017050};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., Dai D.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Pseudomonas sp. HPB0071.";
RL   Submitted (MAR-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:ENA28702.1}.
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DR   EMBL; AQFP01000016; ENA28702.1; -; Genomic_DNA.
DR   RefSeq; WP_010798847.1; NZ_KI517368.1.
DR   AlphaFoldDB; N2IMS3; -.
DR   GeneID; 84594960; -.
DR   PATRIC; fig|1203578.3.peg.4417; -.
DR   HOGENOM; CLU_087854_1_1_6; -.
DR   OrthoDB; 9807202at2; -.
DR   Proteomes; UP000017050; 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:SF1; 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:UP000017050}.
SQ   SEQUENCE   173 AA;  19164 MW;  177982E12A64E212 CRC64;
     MPEPTKIKDV YLKPGELHFG GADTRIRTLL GSCVALVFWH PQRQLGGMCH YLLPTRSKGH
     KVSDRLDGHY GDEALALLLQ AIQMSGTQPS EFTLRVFGGG NMFPGIARNE KDHIGLQNVK
     AAKRLLQAHG LVCSASHVEG IGHRRLSFSI WDGEVKLEQS PPVQAPPRQR DRL
//
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