ID Q5WIW9_SHOC1 Unreviewed; 523 AA. AC Q5WIW9; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 02-SEP-2026, entry version 93. DE SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:BAD63686.1}; DE EC=3.2.1.37 {ECO:0000313|EMBL:BAD63686.1}; DE EC=3.2.1.55 {ECO:0000313|EMBL:BAD63686.1}; GN OrderedLocusNames=ABC1148 {ECO:0000313|EMBL:BAD63686.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63686.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD63686.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63686.1, RC ECO:0000313|Proteomes:UP000001168}; RA Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.; RT "Molecular cloning and nucleotide sequence of the gene for an alkaline RT protease from the alkalophilic Bacillus sp. KSM-K16."; RL J. Ferment. Bioeng. 78:105-108(1994). RN [2] {ECO:0000313|EMBL:BAD63686.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63686.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=7632397; DOI=10.1007/s002530050437; RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., RA Kawai S., Ito S.; RT "Purification and properties of an alkaline protease from alkalophilic RT Bacillus sp. KSM-K16."; RL Appl. Microbiol. Biotechnol. 43:473-481(1995). RN [3] {ECO:0000313|EMBL:BAD63686.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63686.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=9278275; DOI=10.1093/protein/10.6.627; RA Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.; RT "High-resolution crystal structure of M-protease: phylogeny aided analysis RT of the high-alkaline adaptation mechanism."; RL Protein Eng. 10:627-634(1997). RN [4] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD63686.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63686.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=17429572; DOI=10.1007/s00792-007-0074-1; RA Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K., RA Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.; RT "Intragenomic diversity of the V1 regions of 16S rRNA genes in high- RT alkaline protease-producing Bacillus clausii spp."; RL Extremophiles 11:597-603(2007). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}. 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; AP006627; BAD63686.1; -; Genomic_DNA. DR RefSeq; WP_011246001.1; NC_006582.1. DR AlphaFoldDB; Q5WIW9; -. DR STRING; 66692.ABC1148; -. DR PaxDb; 66692-ABC1148; -. DR KEGG; bcl:ABC1148; -. DR eggNOG; COG3507; Bacteria. DR HOGENOM; CLU_016508_2_0_9; -. DR OrthoDB; 9801455at2; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC. 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 Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 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 InterPro; IPR051795; Glycosyl_Hydrlase_43. 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:UP000001168}. FT DOMAIN 324..519 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 188 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 523 AA; 59276 MW; 96BFD6A11D470651 CRC64; MEPFNNPIIP GFYPDPSICR VNEDYYLVTS TFEYFPGVPI FHSTDLVNWR QIGHVLDRPE QLNLDGTPNS RGIYAPTIRY NNGLFYMITT FVESQHGARR NFFVTAKDPA GPWSDPVWIK GAPGIDPSLF FDDDGRVYYT GNRVPPTGQT HAKHMEIWLQ EIDPITGCLL GEPTGIWDGA LKIAHAQEAP HLYKKDGYYY LFIAEGGTGF THAVTVARSR EIAGPYEANR RNPVLTHRHL GQDYPITNVG HADIVQTQDD EWWLVCLGSR PYGGMYRNMG RETFLAPMRW EDDWPVVCPE TGKIEVEMPG PSLPRQKVEP LPVRDDFNAR KLGFQWNMIR TPRTPFYSLE ARKGYLQLNV RPETLADQAN PSFIGRRQQH RSFTVRAFME FDPKQSGEAA GLALFYSQKN HYRFELIRSG QLFIRLVKVE DGVETVAGKS TAPIPATAIE WQVAADLQEL SFSYRVPGGK WRMVANKQDS RLLSTDRAGG FVGTYIGMFA TSNGQNSTTT AAFDWFEYKG EST //