ID EABF_STRCO Reviewed; 475 AA. AC O54161; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=Extracellular exo-alpha-L-arabinofuranosidase; DE Short=ABF; DE EC=3.2.1.55; DE AltName: Full=Arabinosidase; DE AltName: Full=Arabinoxylan arabinofuranohydrolase; DE Flags: Precursor; GN Name=abfB; OrderedLocusNames=SCO5932; ORFNames=SC7H1.02; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). CC -!- FUNCTION: Involved in the degradation of xylan and is a key enzyme in CC the complete degradation of the plant cell wall. It has a specific CC arabinofuranose-debranching activity on xylan from gramineae. Acts CC synergistically with the xylanases and binds specifically to xylan. CC From small arabinoxylo-oligosides (ranging from arabinoxylotriose to CC arabinoxylohexaose), it liberates arabinose and, after prolonged CC incubation, the purified enzyme exhibits some xylanolytic activity as CC well (By similarity). {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 degradation; xylan degradation. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydr olase 62 family. CC {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; AL939125; CAA16189.1; -; Genomic_DNA. DR PIR; T35697; T35697. DR RefSeq; NP_630049.1; NC_003888.3. DR RefSeq; WP_011030541.1; NZ_VNID01000007.1. DR PDB; 3WMY; X-ray; 1.40 A; A=38-475. DR PDB; 3WMZ; X-ray; 1.90 A; A=38-475. DR PDB; 3WN0; X-ray; 1.90 A; A=38-475. DR PDB; 3WN1; X-ray; 2.00 A; A=38-475. DR PDB; 3WN2; X-ray; 2.10 A; A=38-475. DR PDBsum; 3WMY; -. DR PDBsum; 3WMZ; -. DR PDBsum; 3WN0; -. DR PDBsum; 3WN1; -. DR PDBsum; 3WN2; -. DR AlphaFoldDB; O54161; -. DR SMR; O54161; -. DR STRING; 100226.gene:17763592; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GH62; Glycoside Hydrolase Family 62. DR PaxDb; 100226-SCO5932; -. DR PATRIC; fig|100226.15.peg.6029; -. DR eggNOG; COG3693; Bacteria. DR HOGENOM; CLU_041805_2_0_11; -. DR InParanoid; O54161; -. DR OrthoDB; 3317993at2; -. DR PhylomeDB; O54161; -. DR BRENDA; 3.2.1.55; 5998. DR UniPathway; UPA00114; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd08987; GH62; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR005193; GH62_arabinosidase. DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1. DR PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1. DR Pfam; PF03664; Glyco_hydro_62; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Lectin; KW Polysaccharide degradation; Reference proteome; Secreted; Signal; KW Xylan degradation. FT SIGNAL 1..37 FT /evidence="ECO:0000255" FT CHAIN 38..475 FT /note="Extracellular exo-alpha-L-arabinofuranosidase" FT /id="PRO_0000008036" FT DOMAIN 39..166 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 198..208 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 224..229 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:3WMY" FT HELIX 235..240 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 251..258 FT /evidence="ECO:0007829|PDB:3WMY" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 263..281 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 307..314 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 316..324 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 326..336 FT /evidence="ECO:0007829|PDB:3WMY" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:3WMY" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 361..368 FT /evidence="ECO:0007829|PDB:3WMY" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:3WN1" FT STRAND 374..381 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 383..395 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 401..413 FT /evidence="ECO:0007829|PDB:3WMY" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 426..430 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:3WMY" FT HELIX 443..445 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 447..452 FT /evidence="ECO:0007829|PDB:3WMY" FT HELIX 461..463 FT /evidence="ECO:0007829|PDB:3WMY" FT STRAND 467..473 FT /evidence="ECO:0007829|PDB:3WMY" SQ SEQUENCE 475 AA; 50046 MW; 47E707FE543CA60D CRC64; MHRGSLSRGH TSAVLAAVVA ALAALAALLV ATTPAQAAGS GALRGAGSNR CLDVLGGSQD DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA TAPGTRVQIW SCSGGANQQW RVNSDGTVVG VESGLCLEAA GAGTANGTAV QLWTCNGGGN QKWTGLTGTP PTDGTCALPS TYRWSSTGVL AQPKSGWVAL KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS AGQNAMNQAA VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT IMSDTKANLF EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW TPQAASEGNP FAGKANSGAT WTNDISHGDL VRDNPDQTMT VDPCNLQFLY QGKSPNAGGD YNSLPWRPGV LTLRR //