ID   CHED_PYRAB              Reviewed;         163 AA.
AC   Q9UYF7; G8ZIX2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=PYRAB15510;
GN   ORFNames=PAB1335;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50455.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71005.1; -; Genomic_DNA.
DR   PIR; A75002; A75002.
DR   RefSeq; WP_010868668.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYF7; -.
DR   SMR; Q9UYF7; -.
DR   STRING; 272844.PAB1335; -.
DR   EnsemblBacteria; CAB50455; CAB50455; PAB1335.
DR   GeneID; 1495834; -.
DR   KEGG; pab:PAB1335; -.
DR   PATRIC; fig|272844.11.peg.1650; -.
DR   eggNOG; arCOG02380; Archaea.
DR   HOGENOM; CLU_087854_2_0_2; -.
DR   OMA; VGMADLN; -.
DR   OrthoDB; 86566at2157; -.
DR   PhylomeDB; Q9UYF7; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..163
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_0000251096"
SQ   SEQUENCE   163 AA;  17736 MW;  AF126901A86BC35F CRC64;
     MTREIKVGIG DYAVGKGEGI ISTYGLGSCV GITLYDRVTK VGGLLHALLP EAARYGHRGN
     PAKYVDTGLQ LLLKEVLKLG ASKFRLEAKL FGGAQMFQNI KSDELKIGER NVQTAKRELK
     KLGIRLVAED TGGRGGRTIY LDLSTGKVRM RKVIGGQVIE KVY