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Database: UniProt
Entry: I4D890_DESAJ
LinkDB: I4D890_DESAJ
Original site: I4D890_DESAJ 
ID   I4D890_DESAJ            Unreviewed;       263 AA.
AC   I4D890;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative xylanase/chitin deacetylase {ECO:0000313|EMBL:AFM42014.1};
GN   OrderedLocusNames=Desaci_3107 {ECO:0000313|EMBL:AFM42014.1};
OS   Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM42014.1, ECO:0000313|Proteomes:UP000002892};
RN   [1] {ECO:0000313|EMBL:AFM42014.1, ECO:0000313|Proteomes:UP000002892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22704 / JCM 16185 / SJ4
RC   {ECO:0000313|Proteomes:UP000002892};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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DR   EMBL; CP003639; AFM42014.1; -; Genomic_DNA.
DR   RefSeq; WP_014828005.1; NC_018068.1.
DR   AlphaFoldDB; I4D890; -.
DR   STRING; 646529.Desaci_3107; -.
DR   KEGG; dai:Desaci_3107; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_2_9; -.
DR   OrthoDB; 61520at2; -.
DR   Proteomes; UP000002892; Chromosome.
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   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:SF128; POLYSACCHARIDE DEACETYLASE PDAB-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:AFM42014.1};
KW   Glycosidase {ECO:0000313|EMBL:AFM42014.1};
KW   Hydrolase {ECO:0000313|EMBL:AFM42014.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:AFM42014.1};
KW   Xylan degradation {ECO:0000313|EMBL:AFM42014.1}.
FT   DOMAIN          50..235
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   263 AA;  28923 MW;  1733B7760620E336 CRC64;
     MKLIIFRRPS WRNLALWGIL LLVLITYREN VTSVFSGKLK PIYSATVNTP AIGLTFDISW
     GEKTAEPILD ILKREGVHAT FFLSSPWAEK HQALVQRMVA DGHEIGSHGN RHIDLNTLGA
     GEIEQEISSA QQVLERISGR KVRLIRAPNG AYDNKVITVA HKLGYRVIQW SVDSLDWKRP
     GPSAVVNNVL NGIRPGGGAK AGDIILFHAS DSAPDTIQAL PSVLEQLKQK GYTLMPVGKL
     LSEASGTWPP ESKLENETSP SHN
//
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