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Database: UniProt
Entry: U2K623_9FIRM
LinkDB: U2K623_9FIRM
Original site: U2K623_9FIRM 
ID   U2K623_9FIRM            Unreviewed;       344 AA.
AC   U2K623;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=peptidoglycan-N-acetylglucosamine deacetylase {ECO:0000256|ARBA:ARBA00044052};
DE            EC=3.5.1.104 {ECO:0000256|ARBA:ARBA00044052};
GN   ORFNames=RUMCAL_03301 {ECO:0000313|EMBL:ERJ87530.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ87530.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ87530.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ87530.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) 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   -!- 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:ERJ87530.1}.
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DR   EMBL; AWVF01000440; ERJ87530.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2K623; -.
DR   STRING; 411473.RUMCAL_03301; -.
DR   PATRIC; fig|411473.3.peg.2767; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_1_9; -.
DR   OrthoDB; 9806342at2; -.
DR   Proteomes; UP000016662; 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; 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;
FT   DOMAIN          110..284
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          313..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  37313 MW;  91C2AD7476436D5E CRC64;
     MWNKDLKQEI WRGIMQTERR IAKCAVLAAL VLLGGACTKI DAVRSDGKQT QEAVMAAASA
     AEVSTTAETT TAATTETTTT TVTTTVTTTT AAGICQPFID ENANIDPSKP MVALTFDDGP
     GQYTNSILDT LEAYQAHASF FVVGQNINDE TSAVMQRAVG LGCEIGSHTE NHADLVKADA
     NTFQQEIQQA DDRILQAIGR YPYFLRPPYG DFNDDVRRHV GKPLAFWSVD TKDWKTRNTA
     STVSATLNNI EDGDVVLMHD IYGETAAAVA QIVPSLVQQG YQLVTLSELT YYRGVEMENG
     MIVFNMHPAN PNYKLPPDPD VPEPQTTPAP ETETTTETVA AAGQ
//
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