ID A0A0L0BFP7_9MICC Unreviewed; 493 AA.
AC A0A0L0BFP7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KNC18723.1};
GN ORFNames=AC792_10540 {ECO:0000313|EMBL:KNC18723.1};
OS Arthrobacter sp. RIT-PI-e.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC18723.1, ECO:0000313|Proteomes:UP000053253};
RN [1] {ECO:0000313|Proteomes:UP000053253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
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:KNC18723.1}.
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DR EMBL; LGIU01000074; KNC18723.1; -; Genomic_DNA.
DR RefSeq; WP_049830480.1; NZ_LGIU01000074.1.
DR AlphaFoldDB; A0A0L0BFP7; -.
DR STRING; 1681197.AC792_10540; -.
DR PATRIC; fig|1681197.3.peg.1618; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000053253; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF07679; I-set; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000053253};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..493
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005534711"
FT DOMAIN 380..471
FT /note="Immunoglobulin I-set"
FT /evidence="ECO:0000259|Pfam:PF07679"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 263
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 207
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 493 AA; 53003 MW; A0FD75B2C6B68533 CRC64;
MTSRNSHRLR PATIIAALAL ALSGSALPAS AAPPSPTDPP TLTQQSAAGS LKDLVGGKSV
VGETSPIHDP ALVIDDDGTW YVYSTGLVNR ENGGTIQTWS SSDEGTTWEY RGTVWDEIPA
WIDERYSDGV LPENLWAPEI YEHDGTYYLY YSASRFGGNN SLTALATNTT LDPEDPDYAW
VDQGLVVDSP ATGLDPANPG KTFNAIDAGI VEDADGNPYM SIGSFWYGIF LVPLEWPSGK
PVENWQSQTV NIADRFLPGN PIEAPYILHR DGYYYLFTSF DFCCRGADST YKIAVARSTS
VTGPYLDKEG RDMARGGGSI LMESHGAMNG LGGQSVSGDH LAFHYYDAGN AAAPYLPTLG
LQKLGWEDGW PTVDQTVDLP ELVTTPRDVK AREGHKATFL ASATGTPEPV AVWESSDDDG
ATWQPADVTQ RAKRDHRGTY ISIAQVGKAP ASSDGRLYRA TFSNAHGAVT TDPVELSVWT
KPGKPGKPGK PGK
//
