ID A8FDV3_BACP2 Unreviewed; 511 AA. AC A8FDV3; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 87. DE SubName: Full=Arabinoxylan arabinofuranohydrolase {ECO:0000313|EMBL:ABV62420.1}; GN OrderedLocusNames=BPUM_1748 {ECO:0000313|EMBL:ABV62420.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62420.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV62420.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62420.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] {ECO:0000313|EMBL:ABV62420.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62420.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23812891; DOI=10.1007/s00792-013-0559-z; RA Tirumalai M.R., Fox G.E.; RT "An ICEBs1-like element may be associated with the extreme radiation and RT desiccation resistance of Bacillus pumilus SAFR-032 spores."; RL Extremophiles 17:767-774(2013). RN [3] {ECO:0000313|EMBL:ABV62420.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62420.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23799069; RA Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S., RA Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.; RT "Candidate genes that may be responsible for the unusual resistances RT exhibited by Bacillus pumilus SAFR-032 spores."; RL PLoS ONE 8:E66012-E66012(2013). 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; CP000813; ABV62420.1; -; Genomic_DNA. DR RefSeq; WP_012010147.1; NC_009848.4. DR AlphaFoldDB; A8FDV3; -. DR STRING; 315750.BPUM_1748; -. DR PaxDb; 315750-BPUM_1748; -. DR GeneID; 5621009; -. DR KEGG; bpu:BPUM_1748; -. DR eggNOG; COG3507; Bacteria. DR HOGENOM; CLU_009397_11_3_9; -. DR OrthoDB; 9801455at2; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. 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; cd04084; CBM6_xylanase-like; 1. DR CDD; cd09003; GH43_XynD-like; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1. DR InterPro; IPR005084; CBM6. DR InterPro; IPR006584; Cellulose-bd_IV. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR006710; Glyco_hydro_43. DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf. DR InterPro; IPR052176; Glycosyl_Hydrlase_43_Enz. DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1. DR PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1. DR Pfam; PF03422; CBM_6; 1. DR Pfam; PF04616; Glyco_hydro_43; 1. DR SMART; SM00606; CBD_IV; 1. DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS51175; CBM6; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}; KW Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE- KW ProRule:PRU00303}; Xylan degradation {ECO:0000256|ARBA:ARBA00022651}. FT SIGNAL 1..28 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..511 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT /id="PRO_5049680290" FT CHAIN 29..511 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002721073" FT DOMAIN 383..509 FT /note="CBM6" FT /evidence="ECO:0000259|PROSITE:PS51175" FT SITE 190 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" FT LIPID 20 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT LIPID 20 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" SQ SEQUENCE 511 AA; 54499 MW; 04BD8381214EEBF8 CRC64; MRKRMKCGLC FLILALVLSC IPVYDASAAS TPIAKRVGNA NPLIDHHLGA DPFALTYNGR VYIYMSSDDY EYQSNGTIKD NSFANLNRVF VISSADMVNW TDHGAIPVAG ANGANGGKGI AKWAGASWAP AAAVKKINGK DKFFLYFANS GGGIGVLTAD SPIGPWKDPI GKALVTPNTP GMSGVVWLFD PAVFVDDDGT GYLYAGGGVP GGSNPTQGQW ANPKTARVLK LGPDMTSVAG SASTIDAPFM FEDSGMHKYN GTYYYSYCIN FGGSHPADKP PGEIGYMTSS SPMGPFTYKG HFLKNPGSFF GGGGNNHHAV FNFKNEWYVV YHTQTVSSAL YGAGKGYRSP HINKLVHNAD GSLREVAANF EGVKQLSNLN PYQRVEAETF AWNGRILTEA SSAPGGPVNN QHVTNIQNGD WVAVSNVDFG SRGARTFKAN VAAASGGQIE VRLGSPDGRM VGTLNVPSSG GNWREIETTV NGATGVHNVF FVFKGNGANL FQFDSWQFTQ R //