ID T0GYN4_9SPHN Unreviewed; 544 AA.
AC T0GYN4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:EQB05787.1};
GN ORFNames=L286_07520 {ECO:0000313|EMBL:EQB05787.1};
OS Sphingobium sp. HDIP04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=428994 {ECO:0000313|EMBL:EQB05787.1, ECO:0000313|Proteomes:UP000015528};
RN [1] {ECO:0000313|EMBL:EQB05787.1, ECO:0000313|Proteomes:UP000015528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDIP04 {ECO:0000313|EMBL:EQB05787.1,
RC ECO:0000313|Proteomes:UP000015528};
RX PubMed=24051321;
RA Mukherjee U., Kumar R., Mahato N.K., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium sp. Strain HDIPO4, an Avid Degrader
RT of Hexachlorocyclohexane.";
RL Genome Announc. 1:e00749-e00713(2013).
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:EQB05787.1}.
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DR EMBL; ATDO01000073; EQB05787.1; -; Genomic_DNA.
DR RefSeq; WP_020819759.1; NZ_ATDO01000073.1.
DR AlphaFoldDB; T0GYN4; -.
DR PATRIC; fig|428994.3.peg.1429; -.
DR Proteomes; UP000015528; 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 336..535
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 137
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; 60301 MW; AE6BDC043D8A774B CRC64;
MTNISNPILR GFNPDPSILR VGEDFYIATS TFEWYPGVQI HHSRDLVNWR LVARPLERAG
QLDMRGDPDG CGVWAPDLSH ADGRFWLVFT DVKRYGATTV HGAKGMSLRD FPNHVVTCET
IDGIWSDAAH INSSGFDPAL FHDDDGRSWM LNMLWDHRPG RGRFAGIQAQ QLDRATLKLV
GEPTLIFKGT ERGFTEGPHI YKRGGFYHLL VAEGGTGWDH AVVMARSPDL LGPYEVHPDG
AVLTSAGRRD VPIARAGHGD LVELADGSTW LAYLCGRPLP GRERCIMGRE TAIQPMLWGE
DGWLRTVAGD ARPDPSPPAP NLPPASWNAA PWDGRFDDPH LPQDLQWLRS PTPERLFSLR
ERPGFLRLYG RETVGSLFEQ ALVARRQTAF RFTATTSLSF APRSFQQAAG LIHYYNSTKF
YYLCVSAEDG RRQLQLVSAS PENPAGNSLD IMVDALPPDP IDLRADVDGD RLTFAWRADG
EADWHRLPDV HDASILSDEV TLPGLPNFTG AFIGMACQDL SGGGTPADFA SFVYREEEFD
APLD
//
