ID A0A087N7J0_9SPHN Unreviewed; 544 AA.
AC A0A087N7J0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:KFL45093.1};
GN ORFNames=IL54_0461 {ECO:0000313|EMBL:KFL45093.1};
OS Sphingobium sp. ba1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL45093.1, ECO:0000313|Proteomes:UP000029094};
RN [1] {ECO:0000313|EMBL:KFL45093.1, ECO:0000313|Proteomes:UP000029094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT Sphingobium species.";
RL Submitted (JUL-2014) 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:KFL45093.1}.
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DR EMBL; JPPQ01000083; KFL45093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087N7J0; -.
DR PATRIC; fig|1522072.3.peg.4000; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000029094; 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; cd09000; GH43_SXA-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 PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 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.
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}.
FT DOMAIN 338..539
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 145
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 544 AA; 61284 MW; C53245656C8E7559 CRC64;
MDLGAKTGMI SITNPILRGF NPDPSIVRVG DDYYVATSTF EWYPGVQIHH SRDLANWQLV
ARPLRRPAQL DMRGNPDSCG VWAPDLSYAD GRFHLTYTDV KRYGRTTRSD RTDVSLRDFH
NYWVWCDRID GEWSDPVHVN SSGFDPALFH DDDGRSWLLN MLWDHRPGHK RFAGIVIQQM
CLKTGRLLGE RHNIFAGSPL GFTEGPHLYK RDGYYHILVA EGGTERNHAV VMARSRSLFG
PYELHPDGPV LTARDQPDGP LARAGHGDLV ETANGDPWLV YLCGRPLPAS DRCILGRETA
IQPMRWGEDG WLRTIDGTGR PMASVGNVSV ARTLTDDRAD FDDPTLPPPF QWLRTPYPDQ
IFSLTDRSGH LRLFGRESVG SHFTQALVAR RQCEWRFSAE TLVDFHPANF QQSAGLIHYY
NSTKFHYLHI TADDVGQPVI QILSVVPDEA RPSVTSPAIP IARGPVCLRL DVDHETMRFS
YRMADDEAWH EVPGDRDASI LSDEATLPYL PNFTGTFVGM ACQDMAGTGA VADFDYFHYV
ERDG
//
