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Database: UniProt
Entry: D4KZ70_9FIRM
LinkDB: D4KZ70_9FIRM
Original site: D4KZ70_9FIRM 
ID   D4KZ70_9FIRM            Unreviewed;       234 AA.
AC   D4KZ70;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=RO1_21380 {ECO:0000313|EMBL:CBL12660.1};
OS   Roseburia intestinalis XB6B4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL12660.1, ECO:0000313|Proteomes:UP000008953};
RN   [1] {ECO:0000313|EMBL:CBL12660.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12660.1,
RC   ECO:0000313|Proteomes:UP000008953};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Roseburia intestinalis XB6B4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL12660.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12660.1,
RC   ECO:0000313|Proteomes:UP000008953};
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};
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DR   EMBL; FP929050; CBL12660.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4KZ70; -.
DR   KEGG; rix:RO1_21380; -.
DR   PATRIC; fig|718255.3.peg.3306; -.
DR   HOGENOM; CLU_021264_0_1_9; -.
DR   Proteomes; UP000008953; 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   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:CBL12660.1};
KW   Glycosidase {ECO:0000313|EMBL:CBL12660.1};
KW   Hydrolase {ECO:0000313|EMBL:CBL12660.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:CBL12660.1};
KW   Xylan degradation {ECO:0000313|EMBL:CBL12660.1}.
FT   DOMAIN          52..226
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   234 AA;  25938 MW;  4BA2960CC059C8C4 CRC64;
     MREVHNKKIH SYPKDVLIAA VIFAAAVCQW GGNHGKAAET VSFAALEDIA EKKVAITFDD
     GPNPDYTEEL LTGLKERGVN ATFFLLGKEV EKYPEIVKDI SDGGHLIGTH SYEHVNLSNL
     SDAAAIEQVD KTNAAIYDIT GKYPEYIRPP YGCWKCNLDY ETKMIEVLWD VDPKDWATDN
     SGVIAKRVID KVGENDIILL HDASESSVKA AFAIIDELGK EGYTFVTVEE ILME
//
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