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Database: UniProt
Entry: R5IC66_9BACT
LinkDB: R5IC66_9BACT
Original site: R5IC66_9BACT 
ID   R5IC66_9BACT            Unreviewed;       203 AA.
AC   R5IC66;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Putative xylanase/chitin deacetylase {ECO:0000313|EMBL:CCY34512.1};
GN   ORFNames=BN796_01252 {ECO:0000313|EMBL:CCY34512.1};
OS   Alistipes sp. CAG:831.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262698 {ECO:0000313|EMBL:CCY34512.1, ECO:0000313|Proteomes:UP000018094};
RN   [1] {ECO:0000313|EMBL:CCY34512.1, ECO:0000313|Proteomes:UP000018094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:831 {ECO:0000313|Proteomes:UP000018094};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCY34512.1}.
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DR   EMBL; CAYB010000005; CCY34512.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5IC66; -.
DR   STRING; 1262698.BN796_01252; -.
DR   Proteomes; UP000018094; Unassembled WGS sequence.
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   CDD; cd10917; CE4_NodB_like_6s_7s; 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   Carbohydrate metabolism {ECO:0000313|EMBL:CCY34512.1};
KW   Glycosidase {ECO:0000313|EMBL:CCY34512.1};
KW   Hydrolase {ECO:0000313|EMBL:CCY34512.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:CCY34512.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018094};
KW   Xylan degradation {ECO:0000313|EMBL:CCY34512.1}.
FT   DOMAIN          25..203
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   203 AA;  23260 MW;  6ECC7C0044FF0948 CRC64;
     MLIRPPRLLR KIYPSFIWSF PKEKDGIFIT LDDGPCPQVT PWVLDELDRW GAKATFFCIG
     KNVELYPDLF AETVRRGHSV GCHSYSHVPG WGMPVDDYVQ DVDIAAELIR TNLYRPPYAK
     ITVRQAEALS PRYNIVMWNI LSRDYNRKLG HRACARNVVP YLSPGSVIVF HDSKKAAKNL
     WYALPKTLEA AAMKELKCKP IIL
//
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