ID R1HBN5_9GAMM Unreviewed; 256 AA.
AC R1HBN5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01246};
GN ORFNames=G113_06864 {ECO:0000313|EMBL:EOD55844.1};
OS Aeromonas molluscorum 848.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD55844.1, ECO:0000313|Proteomes:UP000013526};
RN [1] {ECO:0000313|EMBL:EOD55844.1, ECO:0000313|Proteomes:UP000013526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=848 {ECO:0000313|EMBL:EOD55844.1,
RC ECO:0000313|Proteomes:UP000013526};
RX PubMed=23788549;
RA Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA Bosch E.;
RT "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT Bivalve Molluscs.";
RL Genome Announc. 1:E00382-13(2013).
CC -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC carbohydrates an important step in the degradation of oligosaccharides.
CC {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01246};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000256|HAMAP-
CC Rule:MF_01246}.
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:EOD55844.1}.
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DR EMBL; AQGQ01000029; EOD55844.1; -; Genomic_DNA.
DR RefSeq; WP_005897032.1; NZ_AQGQ01000029.1.
DR AlphaFoldDB; R1HBN5; -.
DR PATRIC; fig|1268236.3.peg.1364; -.
DR OrthoDB; 9774177at2; -.
DR Proteomes; UP000013526; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd10803; YdjC_EF3048_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR HAMAP; MF_01246; COD; 1.
DR InterPro; IPR022948; COD_ChbG_bac.
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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01246};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01246};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01246};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01246}.
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
SQ SEQUENCE 256 AA; 29048 MW; D6FD5CB5A3B3B82F CRC64;
MHKRLIINAD DFGLCRAQNY GIVEAFEHGV VSSTTAMVTS PAIEHGAWLA TRFPALPIGL
HFVLSWGKPL SPLPCLVNAQ GELDKDIWQK SEGSLLVESE IIQELHQQFD HFVTLFGRAP
SHIDSHHHVH MLPTIYPLVE TFSRQQGIPL RIDRDEVRRH GLTVTDALSC ERFDSRFYGE
QLTREWLLQL LDDADEQGAS SLEIMCHPAF IDLDVQRSSY NLPRLTELAI LTDPALPALI
AERGYRLCSY RDWSPQ
//
