ID   K9IIQ2_DESRO            Unreviewed;       323 AA.
AC   K9IIQ2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000256|ARBA:ARBA00018477};
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA46503.1};
RN   [1] {ECO:0000313|EMBL:JAA46503.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA46503.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of oligosaccharides.
CC       {ECO:0000256|ARBA:ARBA00003451}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00008843}.
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DR   EMBL; GABZ01007022; JAA46503.1; -; mRNA.
DR   AlphaFoldDB; K9IIQ2; -.
DR   OrthoDB; 2912635at2759; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10806; YdjC_like_2; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR006879; YdjC-like.
DR   PANTHER; PTHR31609:SF1; CARBOHYDRATE DEACETYLASE; 1.
DR   PANTHER; PTHR31609; YDJC DEACETYLASE FAMILY MEMBER; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   323 AA;  34612 MW;  E7EF753911AD9E02 CRC64;
     MSWPRVQLVV TADDFGYCPR RDEGIVEAFL SGAVTSVSLL VNGAAADSAA ELARRHQIPI
     GLHANLSEGR PVGPARHSAS SLLGPEGFFL GKMGFREAVA AGDVALSQVR EELEAQLSRF
     QELLGRKPTH VDGHQHVHVL PGVCQVFAEA LQAHGVLFTR LPLERGLGSC TWLEAPARAF
     ACAVERDARA AVGPFSRRGL RWTDIFVGLS TCGRHMSAHR VSGALARALE GTPTGHCLTA
     ELMTHPGYPS VPPAGGCGEG PDAFSCSWER LHELRVLTEP TLQSRLAQDG VQLCALHDLD
     SKRPREGVPG EATLETFLES SQL
//