ID A5FT29_ACICJ Unreviewed; 477 AA. AC A5FT29; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 02-SEP-2026, entry version 74. DE RecName: Full=Xylan 1,4-beta-xylosidase {ECO:0000256|PROSITE-ProRule:PRU10068}; DE EC=3.2.1.37 {ECO:0000256|PROSITE-ProRule:PRU10068}; GN OrderedLocusNames=Acry_3134 {ECO:0000313|EMBL:ABQ28761.1}; OS Acidiphilium cryptum (strain JF-5). OG Plasmid pACRY01 {ECO:0000313|EMBL:ABQ28761.1, OG ECO:0000313|Proteomes:UP000000245}. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Acetobacterales; Acidocellaceae; Acidiphilium. OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ28761.1, ECO:0000313|Proteomes:UP000000245}; RN [1] {ECO:0000313|EMBL:ABQ28761.1, ECO:0000313|Proteomes:UP000000245} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5 {ECO:0000313|Proteomes:UP000000245}; RC PLASMID=Plasmid pACRY01 {ECO:0000313|Proteomes:UP000000245}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.; RT "Complete sequence of plasmid1 pACRY01 of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D- CC xylose residues from the non-reducing termini.; EC=3.2.1.37; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU10068}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. CC {ECO:0000256|ARBA:ARBA00008875}. 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; CP000689; ABQ28761.1; -; Genomic_DNA. DR RefSeq; WP_011930554.1; NC_009467.1. DR AlphaFoldDB; A5FT29; -. DR KEGG; acr:Acry_3134; -. DR HOGENOM; CLU_028597_0_0_5; -. DR Proteomes; UP000000245; Plasmid pACRY01. 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; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1500; Glycosyl hydrolase domain, family 39; 1. DR InterPro; IPR049165; GH39_as. DR InterPro; IPR049166; GH39_cat. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR000514; Glyco_hydro_39. DR InterPro; IPR051923; Glycosyl_Hydrolase_39. DR PANTHER; PTHR12631; ALPHA-L-IDURONIDASE; 1. DR PANTHER; PTHR12631:SF10; BETA-XYLOSIDASE-LIKE PROTEIN-RELATED; 1. DR Pfam; PF01229; Glyco_hydro_39; 1. DR PRINTS; PR00745; GLHYDRLASE39. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABQ28761.1}; KW Plasmid {ECO:0000313|EMBL:ABQ28761.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000245}. FT DOMAIN 15..448 FT /note="Glycosyl hydrolases family 39 N-terminal catalytic" FT /evidence="ECO:0000259|Pfam:PF01229" FT ACT_SITE 158 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR600514-1, FT ECO:0000256|PROSITE-ProRule:PRU10068" SQ SEQUENCE 477 AA; 53805 MW; 02AC2DBA76018BA0 CRC64; MTAMFSSDLS GRTTDFPHFW EHTVGSGHAT LALRADWQAQ LKQAHDELGM RHVRFHGILS DDMGTLVSEG DTFFYSFFNT DQIFDFLLSI GMKPFVELSF MPSALSSGDQ TVFHYRANVG RPRDYAQWAV LIRKLVRHWV DRYGLGEVRQ WFFEVWNEPN LTAFGNGQQS DYFELYRYTV EAIKGVDAML KVGGPATAAN AWIDDFLAFC KANDLPADFV STHHYPTDAF GKPGDDTEAQ LAASTRSILR EQARDVRKNA GDLPVYYTEW CTSSNPRDPM HDDPYAAAFI VKTILEASGL VQGYSYWTFS DIFEENYFPS IPFHGGFGLL NIHGIAKPAY RAFQLLHELG TQMMPVKGSH ATVDAWFVRG DQRSTLVLTN FALPRHPIET EQVSFELKSA KPESMASIQR IDLEHANAKP HWEQRGKPEY LNAATIEELK HLSQFQSEPV PVNGDSGKLN IKVSMPPQSV AAIHFSN //