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Database: UniProt
Entry: B1CAL0_9FIRM
LinkDB: B1CAL0_9FIRM
Original site: B1CAL0_9FIRM 
ID   B1CAL0_9FIRM            Unreviewed;       358 AA.
AC   B1CAL0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:EDS72483.1};
GN   ORFNames=ANASTE_02204 {ECO:0000313|EMBL:EDS72483.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72483.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS72483.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72483.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS72483.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72483.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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:EDS72483.1}.
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DR   EMBL; ABIL02000006; EDS72483.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1CAL0; -.
DR   STRING; 445971.ANASTE_02204; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_773035_0_0_9; -.
DR   OrthoDB; 9806342at2; -.
DR   Proteomes; UP000005178; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd10944; CE4_SmPgdA_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; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF125; POLYSACCHARIDE DEACETYLASE YHEN-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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005178};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..343
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   358 AA;  41004 MW;  CC27FB21B6EBD228 CRC64;
     MNNDLNNSMQ KNLTILFSLI YILMLLVTLN ISSVNNYNKA YENIQSKNEN TFISSKNIKG
     PIKYSKNKED NAITKTVCKI YDSKGELSGY IDNNEKIKII KTKGNKDIIS YANTNKFSIS
     ELLSSMTNKN KDLFTIGEVN KNDIKSRKLK KIYLTFDDGP TKMTYKVLKV LKKNNIKATF
     FFNGAKNNEG KKVVNEIVKE GHLLALHTYS HDYKKVYKSP KAFLKDLEKN RINFLKATGY
     DCRIFRFPGG TNNTVSFSYG GKKVIRKAIK LTKSHGYDYV DWNSFPDDVG AKMPKKQYNR
     IIKQAKWNDE SVVLMHVFDR NTALPKGLDH VIKTLKKQGY TFDTVDNLNT PVKFAPAK
//
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