ID A0A0Q9DCT6_9HYPH Unreviewed; 542 AA. AC A0A0Q9DCT6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 29-SEP-2021, entry version 16. DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KRD53439.1}; GN ORFNames=ASE60_13645 {ECO:0000313|EMBL:KRD53439.1}; OS Ensifer sp. Root278. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer; unclassified Ensifer. OX NCBI_TaxID=1736509 {ECO:0000313|EMBL:KRD53439.1, ECO:0000313|Proteomes:UP000051719}; RN [1] {ECO:0000313|EMBL:KRD53439.1, ECO:0000313|Proteomes:UP000051719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root278 {ECO:0000313|EMBL:KRD53439.1, RC ECO:0000313|Proteomes:UP000051719}; RA Gilbert D.G.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD53439.1, ECO:0000313|Proteomes:UP000051719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root278 {ECO:0000313|EMBL:KRD53439.1, RC ECO:0000313|Proteomes:UP000051719}; RA Schulze-Lefert P.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-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:KRD53439.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LMJJ01000040; KRD53439.1; -; Genomic_DNA. DR RefSeq; WP_057254272.1; NZ_LMJJ01000040.1. DR EnsemblBacteria; KRD53439; KRD53439; ASE60_13645. DR Proteomes; UP000051719; 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 Gene3D; 2.115.10.20; -; 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 Pfam; PF17851; GH43_C2; 1. DR Pfam; PF04616; Glyco_hydro_43; 1. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF75005; SSF75005; 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 333..536 FT /note="GH43_C2" FT /evidence="ECO:0000259|Pfam:PF17851" FT ACT_SITE 16 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1" FT ACT_SITE 195 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1" FT SITE 129 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 542 AA; 61188 MW; 49D7CF742B4057B3 CRC64; MTAMIRNPIL KGFNPDPSIC RVGDDYYIAT STFEWYPGVQ IHHSRDLVNW RLVRRPLERA SQLDMRGNPD SCGVWAPCLS YNDGLFWLVY TDVKRFDGNF KDAHNYIVTA EAIEATWSDP VYVNSSGFDP SLFHDDDGRK WFLNMQWNHR TESFGGSPKH PAFDGILLQE WDERTRKLVG PVKNIFAGSA LGLVEGPHLF KRNGWYYLTT AEGGTGYDHA VTMARSRTID GPYEMHPDTY LMTSKDHPEA PLQRAGHGQY VETPDGQAYH THLCGRPLPP QRRCTLGRET ALQKCVWRDD GWLYLESGGP VPEVLVPAPV QVERIPAATV VETDFNDSAL PIEFQWLRTP APERIFSLEW RPGHLRLFGR ESIGSWFEQA LVARRQEHHA FRAETTADFK AETYQQVAGL THYYNRHKFH ALGITWHETL GRALTILSCP GDFPHGRLEF PVGSGIAIPD GPIDLAMEIR DNDLQFFWRE TRTGDWRAIG PVLDAGVVSD EGGRGEHGSF TGAFAGMFAF DTSGVGKAAD FDHFRYVSLA EG //