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Database: UniProt
Entry: A0A0F0KNC1_9MICO
LinkDB: A0A0F0KNC1_9MICO
Original site: A0A0F0KNC1_9MICO 
ID   A0A0F0KNC1_9MICO        Unreviewed;       522 AA.
AC   A0A0F0KNC1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KJL21954.1};
DE            EC=3.2.1.37 {ECO:0000313|EMBL:KJL21954.1};
GN   Name=xynB_1 {ECO:0000313|EMBL:KJL21954.1};
GN   ORFNames=RL72_02261 {ECO:0000313|EMBL:KJL21954.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL21954.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL21954.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL21954.1,
RC   ECO:0000313|Proteomes:UP000033448};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-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:KJL21954.1}.
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DR   EMBL; JYIT01000079; KJL21954.1; -; Genomic_DNA.
DR   RefSeq; WP_045250941.1; NZ_JYIT01000079.1.
DR   AlphaFoldDB; A0A0F0KNC1; -.
DR   PATRIC; fig|582680.7.peg.2309; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000033448; Unassembled WGS sequence.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18617; GH43_XynB-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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT   DOMAIN          336..512
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        15
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            126
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   522 AA;  56272 MW;  A4C43E82B7A653E5 CRC64;
     MIAAANPILP GCHPDPSICR VGEWYYLVTS TFEYLPGLPV LRSRDLIRWE TVAHVIDRPG
     MLDFDGIGSS GGLYAPTIRH GLGLFWVVCT LVDRDDGSRG GNFLVTASDP AGPWSDPVML
     DAAGIDPSIA FDDEGRVWLH GTRLATAPEW HDQTEVWVRE YAPAERRLVG AEHVIWRGAV
     RGAVWAEGPH LYRVDGRWLL IAAEGGTEFH HAVSAARADE IAGPYAGDRA NPVFTHRQLG
     RTSPVIGAGH ADLVQAADGS WFAVMLAMRA DDGRHYPLGR ETFLCPVVWE DGWPVFAPGE
     GRLPSAVAIP WATEAPRAGS WQPDDRVAGV VAPADPRWTA LRALPAEVAI AEGDVWRLPV
     RAASLHDPSA PAFLGVRQQH ADVDVRCTLD VRGLAEGESA GVVLRQSERD HVAVAVTRTP
     DGLRLTSERC LGGEVLRRDH GAPAEAPEVE LVVSGRGYDY AFRHAGRDLE SADGRDLDAS
     ATGGFLGLWI GAYATSAGAE PSGEVRITRF AYAPAQADHG DR
//
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