ID A0A0X3V9W4_9ACTN Unreviewed; 325 AA.
AC A0A0X3V9W4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:KUL41561.1};
GN ORFNames=ADL15_04760 {ECO:0000313|EMBL:KUL41561.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL41561.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL41561.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL41561.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL41561.1}.
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DR EMBL; LLZH01000013; KUL41561.1; -; Genomic_DNA.
DR RefSeq; WP_067685339.1; NZ_LLZH01000013.1.
DR AlphaFoldDB; A0A0X3V9W4; -.
DR OrthoDB; 9801375at2; -.
DR Proteomes; UP000053244; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10953; CE4_SlAXE_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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 SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007055698"
FT DOMAIN 33..209
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 233..325
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 216..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 33480 MW; B8AEE7BA1FEC6490 CRC64;
MRIAASLAAI VAAAAGIAVT MDATPSQAAA CSGYVGLTYD DGPTAGNTQN LLNTLRANGL
RATMFNEGQY AAANPGLVRA QVDAGMWVGN HSYTHPHLTQ QSQATMDSEI SRTQTAIANA
GGGTPKLFRP PYGETNATLK AVEQKYGLTE IIWDVDSQDW NNASTDAIVA AAGRLTNGQV
ILMHDWPANT VAAVPRIAQG LAARGLCSGM ISPSTGRAVA PDGGGTTTPP TTTPPQSGSC
TATISAGQQW SDRYNLSVAV TGSSSWTVTL NIPSPAKVIA TWNTAATWPS AQQMVAKPNG
SGNTFGVTIQ TNGNWTWPSA SCATA
//
