ID D4JVT3_9FIRM Unreviewed; 207 AA.
AC D4JVT3;
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=EUS_21960 {ECO:0000313|EMBL:CBK97202.1};
OS [Eubacterium] siraeum 70/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK97202.1, ECO:0000313|Proteomes:UP000008803};
RN [1] {ECO:0000313|EMBL:CBK97202.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97202.1,
RC ECO:0000313|Proteomes:UP000008803};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum 70/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK97202.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97202.1,
RC ECO:0000313|Proteomes:UP000008803};
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; FP929044; CBK97202.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JVT3; -.
DR KEGG; esu:EUS_21960; -.
DR PATRIC; fig|657319.3.peg.2606; -.
DR HOGENOM; CLU_021264_0_1_9; -.
DR BioCyc; ESIR657319:G136K-1861-MONOMER; -.
DR Proteomes; UP000008803; 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.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000313|EMBL:CBK97202.1};
KW Glycosidase {ECO:0000313|EMBL:CBK97202.1};
KW Hydrolase {ECO:0000313|EMBL:CBK97202.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:CBK97202.1};
KW Xylan degradation {ECO:0000313|EMBL:CBK97202.1}.
FT DOMAIN 4..182
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 207 AA; 23528 MW; 61A3DEBB34C775C1 CRC64;
MENKYIALTF DDGPNTVTTP QVLEMLKKHN VTGSFFLVGD NINEESARIA RECFEYGCEI
CNHSRTHSAM PQQTSEEIKA EIEYTNDKIK QITGGVAPKF FRPPYIALCD SMYDDIPLTF
ICGNGAEDWL DEISAEERSK RIIDQAQNGM IILLHDMEGN FRTVQALDTI IPELKRQGYT
FVTVSDLFAK CKITPRKRVI YSNVLTD
//
