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CHED_ACICJ
ID   CHED_ACICJ              Reviewed;         190 AA.
AC   A5G222;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Acry_2713;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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}.
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DR   EMBL; CP000697; ABQ31904.1; -; Genomic_DNA.
DR   RefSeq; WP_007424129.1; NC_009484.1.
DR   AlphaFoldDB; A5G222; -.
DR   SMR; A5G222; -.
DR   STRING; 349163.Acry_2713; -.
DR   EnsemblBacteria; ABQ31904; ABQ31904; Acry_2713.
DR   KEGG; acr:Acry_2713; -.
DR   eggNOG; COG1871; Bacteria.
DR   HOGENOM; CLU_087854_0_1_5; -.
DR   OMA; RIGGMCH; -.
DR   OrthoDB; 1863047at2; -.
DR   Proteomes; UP000000245; 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..190
FT                   /note="Probable chemoreceptor glutamine deamidase CheD"
FT                   /id="PRO_1000184918"
SQ   SEQUENCE   190 AA;  20278 MW;  2B95135A559450A4 CRC64;
     MTPVAAASPD YARRINIVQG EHRVEHDPEA VLCTILGSCV AACLWDPGAS VGGMNHFLLP
     GDAHAQAGGG GAAMRYGAYA MELLINDLLR HGARRDRLKA KLFGGACLMK GLTDIGRLNA
     DFAERFLAAE GIEIVGGSLR GERGRRIQFW PVSGRARQTL LAADQPALLR AEPDLRTLRA
     PPPSGAVELF
 
 
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