ABFA_ASPNC
ID ABFA_ASPNC Reviewed; 628 AA.
AC A2Q7E0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable alpha-L-arabinofuranosidase A;
DE Short=ABF A;
DE Short=Arabinosidase A;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=abfA; ORFNames=An01g00330;
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. Acts only on
CC small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By
CC 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 metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 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; AM269950; CAK43424.1; -; Genomic_DNA.
DR RefSeq; XP_001388482.1; XM_001388445.1.
DR AlphaFoldDB; A2Q7E0; -.
DR SMR; A2Q7E0; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR PaxDb; A2Q7E0; -.
DR EnsemblFungi; CAK43424; CAK43424; An01g00330.
DR GeneID; 4978177; -.
DR KEGG; ang:ANI_1_42014; -.
DR VEuPathDB; FungiDB:An01g00330; -.
DR HOGENOM; CLU_010060_1_1_1; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
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:0019566; P:arabinose metabolic process; ISS:UniProtKB.
DR GO; GO:2000895; P:hemicellulose catabolic process; IDA:AspGD.
DR GO; GO:0046373; P:L-arabinose metabolic process; IDA:AspGD.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..628
FT /note="Probable alpha-L-arabinofuranosidase A"
FT /id="PRO_5000219287"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 67948 MW; D2961CCBB4195041 CRC64;
MVAFSALSGV SAVSLLLSLV QNAHGISLKV STQGGNSSSP ILYGFMFEDI NHSGDGGIYG
QMLQNPGLQG TAPNLTAWAA VGDATIAIDG DSPLTSAIPS TIKLNIADDA TGAVGLTNEG
YWGIPVDGSE FHSSFWIKGD YSGDITVRLV GNYTGTEYGS TTITHTSTAD NFTQASVKFP
TTKAPDGNVL YELTVDGSVA AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLDDMKGSFL
RFPGGNNLEG NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP
VLGVWDGFAL ESGGNTPLTG DALTPYIDDV LNELEYILGD TSTTYGAWRA ANGQEEPWNL
TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA STSEADCLPE SMPEGSWVDY
HDYSTPDGLV GQFNYFDNLN RSVPYFIGEY SRWEIDWPNM KGSVAEAVFM IGFERNSDVV
KMAAYAPLLQ LINSTQWTPD LIGYTQSPGD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF
GPLYWVASSA GDSYYMKLAN YGSETQDLTV SIPGTSTGKL TVLADSDPDA YNSDTQTLVT
PSESTVQASN GTFTFSLPAW AVAVLAAN
