ABFB_ASPNC
ID ABFB_ASPNC Reviewed; 499 AA.
AC A2R511;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=An15g02300;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
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DR EMBL; AM270337; CAK42333.1; -; Genomic_DNA.
DR RefSeq; XP_001396769.1; XM_001396732.2.
DR AlphaFoldDB; A2R511; -.
DR SMR; A2R511; -.
DR CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
DR PaxDb; A2R511; -.
DR EnsemblFungi; CAK42333; CAK42333; An15g02300.
DR GeneID; 4987831; -.
DR KEGG; ang:ANI_1_372134; -.
DR VEuPathDB; FungiDB:An15g02300; -.
DR HOGENOM; CLU_029332_3_0_1; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:AspGD.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0031221; P:arabinan metabolic process; IC:AspGD.
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 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; PTHR39447; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; SSF110221; 1.
DR SUPFAM; SSF49899; SSF49899; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..499
FT /note="Probable alpha-L-arabinofuranosidase B"
FT /id="PRO_5000221024"
FT REGION 19..335
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 336..499
FT /note="ABD"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT SITE 176..177
FT /note="Cis-peptide bond"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..31
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 81..86
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 176..177
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 401..439
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ SEQUENCE 499 AA; 52509 MW; F1F6C21F601419C9 CRC64;
MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT
TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDVDGYDNL
ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE ATGTATGDEP EGMYAVLDGT HYNDACCFDY
GNAETSSTDT GAGHMEAIYL GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS
YSFVTAAVKG GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN
GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV SLRVTTPGYT
TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE
LLLNANDGTK QFHEDATFCP QAPLNGEGTS LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD
SKTSFNNDVS FEIETAFAS
