GenomeNet

Database: UniProt
Entry: D4JBS7_9FIRM
LinkDB: D4JBS7_9FIRM
Original site: D4JBS7_9FIRM 
ID   D4JBS7_9FIRM            Unreviewed;       300 AA.
AC   D4JBS7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=CC1_32590 {ECO:0000313|EMBL:CBK81798.1};
OS   Coprococcus catus GD/7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81798.1, ECO:0000313|Proteomes:UP000008798};
RN   [1] {ECO:0000313|EMBL:CBK81798.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81798.1,
RC   ECO:0000313|Proteomes:UP000008798};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Coprococcus catus GD/7.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK81798.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81798.1,
RC   ECO:0000313|Proteomes:UP000008798};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC         glucosamine + acetate.; EC=3.5.1.104;
CC         Evidence={ECO:0000256|ARBA:ARBA00043715};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP929038; CBK81798.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JBS7; -.
DR   STRING; 717962.CC1_32590; -.
DR   KEGG; cct:CC1_32590; -.
DR   PATRIC; fig|717962.3.peg.3129; -.
DR   HOGENOM; CLU_021264_0_1_9; -.
DR   Proteomes; UP000008798; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10954; CE4_CtAXE_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:CBK81798.1};
KW   Glycosidase {ECO:0000313|EMBL:CBK81798.1};
KW   Hydrolase {ECO:0000313|EMBL:CBK81798.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:CBK81798.1};
KW   Xylan degradation {ECO:0000313|EMBL:CBK81798.1}.
FT   DOMAIN          87..269
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   300 AA;  33540 MW;  7547146F8FC3D68D CRC64;
     MKSLKKLAGM IGIVILLCGI MTGCSGKRLY SEEELTQIHD VVGAVEQITK EFQYVIGGSI
     QSLLEDSSSR ADLMDYVSTR KYDPDKKIIA LTFDDGPSTD ETNGTSDLLD LLEQYDSKAT
     FFCLGNRLND ESAPLLKRMV ELGCEIGNHS YDHAQLTKLD AKGVRDEIDT TNELIKKYSG
     RDCRIIRPPY GAADNDIVPT NVSQPFIMWD MDTLDWKTKN AASVISLVEK YKEQDWDGAV
     ILMHDIHPTT IEACKTIIPE LVNDGYQLVT VSELAYLKGV KLEPGKSYWG IDEKSTETDY
//
DBGET integrated database retrieval system