ABFC_ASPFU
ID ABFC_ASPFU Reviewed; 505 AA.
AC Q4WTB3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 84.
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=AFUA_1G09900;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAL90319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000004; EAL90319.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_752357.1; XM_747264.1.
DR AlphaFoldDB; Q4WTB3; -.
DR SMR; Q4WTB3; -.
DR STRING; 746128.CADAFUBP00000916; -.
DR GeneID; 3510568; -.
DR KEGG; afm:AFUA_1G09900; -.
DR VEuPathDB; FungiDB:Afu1g09900; -.
DR eggNOG; ENOG502QRW4; Eukaryota.
DR HOGENOM; CLU_017810_1_0_1; -.
DR InParanoid; Q4WTB3; -.
DR OrthoDB; 321051at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000002530; Chromosome 1.
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 GO; GO:0000272; P:polysaccharide catabolic process; IBA:GO_Central.
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_0000394613"
FT CARBOHYD 81
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 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 56572 MW; 268CFE679CC4AA82 CRC64;
MTTFTKLSEQ ETPSISVHAS RRISKINPNI YAGFTEHMGR CIYGGIYDPG NPLSDENGFR
KDVLEALKEL NIPVIRYPGG NFTATYHWID GVGPKDQRPA RPELAWLGTE TNHFGTDEFM
KWCELLGTEP YFCLNFGTGT LDEALAWVEY CNGTKDTYYA NLRRKNGREE PYNIKYWALG
NEVWGPWQVA QMTKEEYAHK AYQWAKALKL LDPSLKLILC GQDGTASWDY YTLKQCLLPA
HSPLSTSTVP LIDMHSIHMY TCGSTHLPNV TAPLAAERAI EITSSLIDLA MIENGIPPDQ
PRPTICFDEW NVWDPLRAEG SKGAEESYTL SDALAVAIWL NVFVRKSKDV GMACIAQSVN
VISPLMTTKD GIIKQTIWWP LYLFSKYMRG WTINAHVSCG AYEGETSPKW IRAVKDTPWL
DVSATLGEDG YANVAVVNIS DEKDMECKFE GATGDVTVFT VTGDSVSACN MKGKEEVGLT
ESTWDGKGAY KFPRHSLTLL RWKAE
