ID   G2FVB2_9FIRM            Unreviewed;       419 AA.
AC   G2FVB2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=DOT_3721 {ECO:0000313|EMBL:EGW38441.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW38441.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW38441.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW38441.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
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   -!- 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:EGW38441.1}.
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DR   EMBL; AGAF01000167; EGW38441.1; -; Genomic_DNA.
DR   RefSeq; WP_009620791.1; NZ_AGAF01000167.1.
DR   AlphaFoldDB; G2FVB2; -.
DR   PATRIC; fig|913865.3.peg.3374; -.
DR   eggNOG; COG0726; Bacteria.
DR   OrthoDB; 61520at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
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;
FT   DOMAIN          40..225
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   419 AA;  49312 MW;  45660F439677F139 CRC64;
     MSLGYMLLSF VLGLLALYTV IPDLLLHRLG IGSWKRQFSP GVALTFDDGP DPEFTPQVLE
     VLRKHQVCAT FFVVAEKAKE FPELIRRIKD EGHLIGVHSL NHRYAWFASP WRTSQEWTES
     VRILERLWED RITWMRPPWG TFNLMTWWWL KRHKMRAVSW NAEGHDWEAR RTPEEITERI
     LKDTNEGTII VLHDSGGEFG ARKNSILALE RLCEQIVREL KLPIVPLEFP DWKLGKRLTF
     RVWEKWEHYY AKRHSVERID AANIFRLEKS MYGGPKLHAE DGQILAEKGD LVAEIHFDNI
     RLQAKGQDMQ QTALKAMHQV RESLPGLARY VAQERTYDNI KVFVAQTLFH RGVKRFGFNV
     QDLPDTLKNR GIVWLQKMIM RVYHPAGKNR NNERLGNKTM LVWISKEKLE RIFEFDYGE
//