ID A0A0N1LQ39_9SPHN Unreviewed; 529 AA.
AC A0A0N1LQ39;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:KPF90856.1};
GN ORFNames=IP81_14525 {ECO:0000313|EMBL:KPF90856.1};
OS Novosphingobium sp. AAP83.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF90856.1, ECO:0000313|Proteomes:UP000037998};
RN [1] {ECO:0000313|EMBL:KPF90856.1, ECO:0000313|Proteomes:UP000037998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF90856.1,
RC ECO:0000313|Proteomes:UP000037998};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF90856.1}.
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DR EMBL; LJHY01000023; KPF90856.1; -; Genomic_DNA.
DR RefSeq; WP_054108717.1; NZ_LJHY01000023.1.
DR AlphaFoldDB; A0A0N1LQ39; -.
DR STRING; 1523425.IP81_14525; -.
DR PATRIC; fig|1523425.4.peg.2323; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000037998; 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; cd09002; GH43_XYL-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF2; XYLOSIDASE_ARABINOSIDASE; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000037998}.
FT DOMAIN 348..517
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 529 AA; 58579 MW; 8E45E1FC043E1224 CRC64;
MTMDRRDALK TAALLGVGLS TPTFATSAPL FATKRGLDNQ RIADLGNGTF RNPVLSGDRP
DPAILKDGAD YYLTFSSFES YPGLLIWHSR DLVNWQPRKP ALHQNIGSVW AVSLEKHNGR
YFLYIPVKAL PQNDIFVITA DHIDGPWTDP IPLGIHTHID PCHTVGEDGT RWLFLSGGDR
VRLSDDGLRT IGAVEHVYDP WRYPAEWDVE GFSPEGPKIH RIGQWFYMIT AVGGTAGPPT
GHMVIAARSR SIHGPWQQHP GNPLVRTTDI GEAWWSRGHA SLVEAPDGSW WSFYHGFENG
FWTLGRQCLL DPVKWTRDGW FHMTGGDLSA PIRKPAGGTA LPHGMALTDT FATLQLGTKW
SFFRPAADEA ARVRVAGNTL YLKGKGLAPS SGSPLLLIAG DTSYQFECDI ELSPGATAGL
VLFYDDKLYA GLGFDAARFV THQYGIERGR PANPHGAKLR MRVVNRRHIV SYYTSGDHGQ
TWVKFDRGME VSGYHHNVRG GFLMLRPGLY AVGPGETKFR NFTFTALDD
//
