ID A0A0E3ZXY5_9BACT Unreviewed; 365 AA.
AC A0A0E3ZXY5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:AKD56490.1};
GN ORFNames=SD10_17830 {ECO:0000313|EMBL:AKD56490.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD56490.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD56490.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD56490.1,
RC ECO:0000313|Proteomes:UP000033054};
RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT isolated from gamma ray-irradiated soil.";
RL Curr. Microbiol. 69:286-291(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP010429; AKD56490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3ZXY5; -.
DR STRING; 1379870.SD10_17830; -.
DR KEGG; srd:SD10_17830; -.
DR PATRIC; fig|1379870.5.peg.3861; -.
DR HOGENOM; CLU_009397_4_1_10; -.
DR Proteomes; UP000033054; Chromosome.
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; cd18619; GH43_CoXyl43_like; 1.
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; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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:UP000033054};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 172
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 365 AA; 40405 MW; 8F83EF624E8DBA11 CRC64;
MFVCLVSGVG LGACQSDKAK QENGEKTSSA SDSADSTQAL SKPLVSHIYT ADPSAHVFNG
KIYIYPSHDI DAGVKEDDEG AHFAMRDYHI LSMDSINGSV TDHGVGLDIK DIPWAGRQLW
APDAAYKNGT YYLYFPVKDK KDVFRMGVAT SKSPSGPFKA EPTPIEGSFS IDPAVFTDTD
GQSYMYFGGI WGGQLQRWAT GKYAANGSKT DSGNDKEPAL SPKVARMSKD MLHFDAPAKD
LKILDKEGKP LLTGDHDRRF FEGGWMHKYN GKYYFSYSTG DTHYLAYAIG NSPEGPFTYQ
GVFMTPVKGW TTHHSIVEFK GRWYIFYHDT ELSGKTHLRN IKVAELVHKA DGTIEPINPY
PAKKM
//
