ID ABFB_ASPTN Reviewed; 506 AA. AC Q0CEE5; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Probable alpha-L-arabinofuranosidase B; DE Short=ABF B; DE Short=Arabinosidase B; DE EC=3.2.1.55; DE Flags: Precursor; GN Name=abfB; ORFNames=ATEG_07939; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., RA Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of CC arabinoxylan, a major component of plant hemicellulose. Able to CC hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L- CC arabinofuranosyl oligosaccharides, but also in polysaccharides CC containing terminal non-reducing L-arabinofuranoses in side chains, CC like L-arabinan, arabinogalactan and arabinoxylan (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside CC residues in alpha-L-arabinosides.; EC=3.2.1.55; CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and CC a C-terminal arabinose-binding domain (ABD). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}. 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; CH476604; EAU32201.1; -; Genomic_DNA. DR RefSeq; XP_001216560.1; XM_001216560.1. DR AlphaFoldDB; Q0CEE5; -. DR SMR; Q0CEE5; -. DR STRING; 341663.Q0CEE5; -. DR GlyCosmos; Q0CEE5; 2 sites, No reported glycans. DR EnsemblFungi; EAU32201; EAU32201; ATEG_07939. DR GeneID; 4322793; -. DR VEuPathDB; FungiDB:ATEG_07939; -. DR eggNOG; ENOG502QS3Q; Eukaryota. DR HOGENOM; CLU_029332_3_0_1; -. DR OMA; WNYPTRY; -. DR OrthoDB; 2573673at2759; -. DR UniPathway; UPA00667; -. DR Proteomes; UP000007963; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; ISS:UniProtKB. DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019566; P:arabinose metabolic process; ISS:UniProtKB. DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat. DR InterPro; IPR038964; ABFB. DR InterPro; IPR007934; AbfB_ABD. DR InterPro; IPR036195; AbfB_ABD_sf. DR InterPro; IPR013320; ConA-like_dom_sf. DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1. DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1. DR Pfam; PF05270; AbfB; 1. DR Pfam; PF09206; ArabFuran-catal; 1. DR SUPFAM; SSF110221; AbfB domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal; Xylan degradation. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..506 FT /note="Probable alpha-L-arabinofuranosidase B" FT /id="PRO_0000394608" FT REGION 27..343 FT /note="Catalytic" FT /evidence="ECO:0000250" FT REGION 344..506 FT /note="ABD" FT /evidence="ECO:0000250" FT ACT_SITE 229 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 305 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 304 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 424 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 427 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 443 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 471 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 476 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT BINDING 496 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT SITE 184..185 FT /note="Cis-peptide bond" FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 375 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 29..39 FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT DISULFID 89..94 FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT DISULFID 184..185 FT /evidence="ECO:0000250|UniProtKB:Q8NK89" FT DISULFID 409..447 FT /evidence="ECO:0000250|UniProtKB:Q8NK89" SQ SEQUENCE 506 AA; 52197 MW; 10913205A0B91DE1 CRC64; MLLPRGFNRA VVTALGVVGT GTLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGPLYQV KRGSDGATTN IAPLSAGGVA NAAAQDSFCA GTTCLITIIY DQSGRGNHLT QAPPGGFKGP EANGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAS GTATGDAPEG MYAVLDGTHY NGGCCFDYGN AETSSTDTGN GHMEAIYFGD NTVWGSGSGS GPWIMADLEN GLFSGSSTKN NAGDPSVSYR FLTAIVKGKP NQWAIRGANA ASGSLSTYYN GARPNASGYN PMSKEGAIIL GIGGDNSIGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YAVAPLTSGP SLTVGSSISL RATTSCCTTR YLAHNGSTVN TQVVSSSSST ALKQQASWTV RAGLANSACF SFESKDTPGS FIRHYDFVLQ LSANDGTKQF YEDATFCPQS GLNGQGSSIR SWNYPTRYFR HYNNVLYAAS NGGVHTFDAT GSFNDDVSWV VSTSFA //