ID A0A0B2A1T6_9MICO Unreviewed; 504 AA.
AC A0A0B2A1T6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Xylan 1,4-beta-xylosidase {ECO:0000313|EMBL:KHK97444.1};
GN ORFNames=LK09_11805 {ECO:0000313|EMBL:KHK97444.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK97444.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK97444.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK97444.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-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:KHK97444.1}.
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DR EMBL; JTDK01000010; KHK97444.1; -; Genomic_DNA.
DR RefSeq; WP_039399465.1; NZ_JTDK01000010.1.
DR AlphaFoldDB; A0A0B2A1T6; -.
DR STRING; 1348253.LK09_11805; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000031030; 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; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF2; XYLOSIDASE_ARABINOSIDASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030}.
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 132
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 504 AA; 55349 MW; B2A26B2C52306C08 CRC64;
MTVSARTAAD LGDGRFRNPV LPGDRPDPSV LRVGDEYFLT YSSFDAAPGL PIWRSPDLVN
WTFVTCALAK PLSTVFAPDF VEHDGRYYIY IPFIPSAWSD AIDSPQVWVI HADAPEGPWS
EPVSTGVSGA IDPGHIVGED GERYLFVSGI RRCRLDAAGL RAVTELEPAY DGWCYPDEWV
TEAYALEGPK LFRRGDWFYL VSAVGGTGGP ATGHMVIVAR SRSVLGPWEN APANPIARTW
TADETWWSRG HATILPGPGD EWHMVSHGYE NGYRTLGRQA LLEPIEWTED GWPIAPARDV
GAVQAKPGPR TAPVAVPAPS DDFTEPAWGE RWVFDNPGRD EAARASFAEG LALRGKGTGP
ADSSPLTTWS MDRAYEVEVE LEVDGAAQGG LLLYFNDRLF YGMGWDGAEM HSYAGGIRTH
WREPSQPGSS IHLRLRNDHH IVTGWHRAPG AEWVRHGVRY DTSGAHSATI NDLKSLRPAL
FAAGDGGVVF RRFRYRALPT ETVA
//
