CHED1_SHEON
ID CHED1_SHEON Reviewed; 206 AA.
AC Q8EF62;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 93.
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}; Synonyms=cheD-1;
GN OrderedLocusNames=SO_2125;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55172.2; -; Genomic_DNA.
DR RefSeq; NP_717728.2; NC_004347.2.
DR RefSeq; WP_011072188.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EF62; -.
DR SMR; Q8EF62; -.
DR STRING; 211586.SO_2125; -.
DR PaxDb; Q8EF62; -.
DR KEGG; son:SO_2125; -.
DR PATRIC; fig|211586.12.peg.2041; -.
DR eggNOG; COG1871; Bacteria.
DR HOGENOM; CLU_087854_0_0_6; -.
DR OrthoDB; 1863047at2; -.
DR PhylomeDB; Q8EF62; -.
DR BioCyc; SONE211586:G1GMP-1955-MON; -.
DR Proteomes; UP000008186; 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..206
FT /note="Probable chemoreceptor glutamine deamidase CheD 1"
FT /id="PRO_0000251064"
SQ SEQUENCE 206 AA; 23314 MW; 3624BD824956963D CRC64;
MVKPSLEFAL NEPNRYYDRH FERSAVKILP GEYFATRENT MIVTVLGSCV AVCLYDPVLK
IGGMNHFLLP NDNVTAPNMM TESARYGVFA MELLINHVLK LGARRNALEA KVFGGGNVLR
GLTVQNIGER NAEFVLDYLQ MEQIPVIAAD LLDIYPRKVY FFPETGLVKV RKIKTIHNST
IMDRESEYRL RIKNLPSGGD VELFGE