ID A0A1Y2R8F2_9BACT Unreviewed; 449 AA.
AC A0A1Y2R8F2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:OSZ77009.1};
GN ORFNames=CAP36_11315 {ECO:0000313|EMBL:OSZ77009.1};
OS Chitinophagaceae bacterium IBVUCB2.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX NCBI_TaxID=1985174 {ECO:0000313|EMBL:OSZ77009.1, ECO:0000313|Proteomes:UP000194400};
RN [1] {ECO:0000313|EMBL:OSZ77009.1, ECO:0000313|Proteomes:UP000194400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVUCB2 {ECO:0000313|EMBL:OSZ77009.1,
RC ECO:0000313|Proteomes:UP000194400};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:OSZ77009.1}.
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DR EMBL; NFUV01000002; OSZ77009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2R8F2; -.
DR STRING; 1985174.CAP36_11315; -.
DR InParanoid; A0A1Y2R8F2; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000194400; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000194400};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..449
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012824757"
FT DOMAIN 324..449
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 161
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 449 AA; 50429 MW; AEE8804C66B20069 CRC64;
MKKNLLQYLS AVLVVLLAVK AEAQNPIIRN QFTADPSARV FGDRVYVYPS HDILATEGKG
RVGWFCMEDY HVFSSSNLSD WTDHGMIVTQ NKVQWVRPDS YSMWAPDCIE RNGKYYFYFP
TAAKDTVAHG RGFTIGVAVA DKPEGPFIPE ATPIKGIRGI DPNVFIDKDG QAYIYWSAGN
IYGAKLKANM LELDSKIDTL GELPTKGLKE GPYMFERKGI YYLTYPHVEN KIERLEYAIG
DNPLGPFKFT GVIMDESASG CWTNHQSIMQ FKKQWYLFYH DRDYSPRFDK ARSIRIDSLF
FNDDGTIKKV TPTLRGVGLT NANQKIQIDR YTQLSGSGVA IDFLDTLDRF KGWKTTFTSS
GAWAQYNSVD FGKKSAKAVT INAQSEKGGI IQLRVNSVNG PLLAEVKIAG GNNWITTKKT
ISKSQNGVQH LFVVSKTDSP VAIDWVSFE
//
