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Database: UniProt
Entry: K4L203_9FIRM
LinkDB: K4L203_9FIRM
Original site: K4L203_9FIRM 
ID   K4L203_9FIRM            Unreviewed;       421 AA.
AC   K4L203;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=DCF50_p590 {ECO:0000313|EMBL:AFV04596.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV04596.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV04596.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV04596.1};
RX   PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA   Tang S., Gong Y., Edwards E.A.;
RT   "Semi-automatic in silico gap closure enabled de novo assembly of two
RT   dehalobacter genomes from metagenomic data.";
RL   PLoS ONE 7:E52038-E52038(2012).
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; CP003870; AFV04596.1; -; Genomic_DNA.
DR   RefSeq; WP_015042603.1; NC_018867.1.
DR   AlphaFoldDB; K4L203; -.
DR   STRING; 1131462.DCF50_p590; -.
DR   KEGG; dec:DCF50_p590; -.
DR   PATRIC; fig|1131462.4.peg.600; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_046845_0_0_9; -.
DR   Proteomes; UP000000482; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10959; CE4_NodB_like_3; 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   Reference proteome {ECO:0000313|Proteomes:UP000000482}.
FT   DOMAIN          41..226
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   421 AA;  47943 MW;  53DDF9F851E094EE CRC64;
     MSTTLLCAFI VAISVFAVYT LIPELFVHFF GIGSWKRHYS PGVTLTFDDG PDPRYTPRFL
     AVLAEQNVQA CFFLVAEKAE KQPELVKSIL DHGHIIGSHG YRHRHAWLMP PLKTWNLWNK
     AMEEMHRLTG QEPVYVRAPW GGVNLSFLFW CHFKGKKLIS WSADGRDWRI ERTPDHIMQK
     ITGLTKEGTI VLLHDSGGDE GAPENTLAAL KPLIMKIQKE RKLPLVPLQL PDWSLPKRIG
     FRVWEKWEHF YAQRKQITRI DERNIFRLGL TRYHGPDLFN ENGELIASAG DLVGEIHLDN
     TRFQSLGANI QKIGYNALKQ ARLSLPVLAS YISLNPGYKD IKVFLGVTLI NRGVKGLGFN
     VTEYTNGNAG FIGFMQKIVY RVYNPSAKKD TERLGTKPKV VWISKDALLE KYLTKKSSTQ
     G
//
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