ABFC_ASPNC
ID ABFC_ASPNC Reviewed; 505 AA.
AC A2QQ94;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Probable alpha-L-arabinofuranosidase C;
DE Short=ABF C;
DE Short=Arabinosidase C;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=abfC; ORFNames=An08g01710;
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}.
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DR EMBL; AM270160; CAK39851.1; -; Genomic_DNA.
DR RefSeq; XP_001392290.1; XM_001392253.1.
DR AlphaFoldDB; A2QQ94; -.
DR SMR; A2QQ94; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR PaxDb; A2QQ94; -.
DR EnsemblFungi; CAK39851; CAK39851; An08g01710.
DR GeneID; 4982486; -.
DR KEGG; ang:ANI_1_1698074; -.
DR VEuPathDB; FungiDB:An08g01710; -.
DR HOGENOM; CLU_017810_1_0_1; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006706; Chromosome 8R.
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:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..505
FT /note="Probable alpha-L-arabinofuranosidase C"
FT /id="PRO_0000394614"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 56636 MW; 3ACDD463A8BB24AE CRC64;
MTTFTKLSDQ DAPSISIHPA RRLSKINPNI YAGFTEHMGR CIYGGIYDPG NSLSDENGFR
KDVLEALKEL NIPVVRYPGG NFMATYHWID GVGPKEKRPA RPELAWLGTE TNQFGTDEFL
KWCEVLGTEP YFCLNFGTGT LDEALAWVEY CNGTKDTYYA NLRRKNGREE PYNVKYWALG
NETWGPWQVE QMTKEAYAHK AYQWAKALKL LDPSLILILC GQDGTASWDY YTLKQCLLPA
HSPLSTSTVP LIDMHSIHLY TSSPSHLPNV TAPLAAERAI EITSSLIDLA RIENGVPPDQ
HRPTICFDEW NVWDPIRAEG SKGAEESYTL SDALAVAVFL NVFVRKSKDL GMACIAQSVN
VISPLMTSKD GITKQTTYWP LYLFSKYMRG WTISVHLSCA SYEGETSPKW VRGVKDTPWL
DVSATLGEDG YVNVAVVNIH EEKDIRSSID GPSGTVSVFT VTGERVQACN MNGKEEVAVT
ESTWEAREQF VFPKHSLTLL RWKLA