ABFA_ASPTN
ID ABFA_ASPTN Reviewed; 628 AA.
AC Q0CTV2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=ATEG_02882;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36156.1; -; Genomic_DNA.
DR RefSeq; XP_001212060.1; XM_001212060.1.
DR AlphaFoldDB; Q0CTV2; -.
DR SMR; Q0CTV2; -.
DR STRING; 341663.Q0CTV2; -.
DR EnsemblFungi; EAU36156; EAU36156; ATEG_02882.
DR GeneID; 4317643; -.
DR VEuPathDB; FungiDB:ATEG_02882; -.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_1_1_1; -.
DR OMA; LYGFMFE; -.
DR OrthoDB; 366915at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; ISS:UniProtKB.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019566; P:arabinose metabolic process; ISS:UniProtKB.
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..25
FT CHAIN 26..628
FT /note="Probable alpha-L-arabinofuranosidase A"
FT /id="PRO_0000394600"
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 164
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 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 68046 MW; 574064EADFD9BB18 CRC64;
MVAFSTISGL GALSLLFSII ESVDGVSLKV STDGGNSSSP LLYGFMFEDI NHSGDGGIYG
QMIQNNGLQG SSPNLTAWAS VGDGTISVDT TNPLTAAIPN SLKLDIKPDA TGAVGFTNEG
YWGIPVDGTE FQNSFWMKGD FSGEITVRLV GNETGTEYGS TTFNQSSSSD DYTKVSVKFP
TTKAPDGNVL YELTVDGESA QGSSLSFTLF ELFAQTYKSR SNGLKPQLAD ALESVKGSFL
RFPGGNNLEG NDVETRWKWN ETIGPLENRP GHQGTWGYFN TDGLGLDEYL YWCEDMNLTP
VLGVWAGFAL ESGGNTPITG DALTPYIEDV LNELEYVLGD PSTTYGKLRA SYGREEPWNV
TLVEIGNEDN LGGGCESYAE RFTAFYNAIH DAYPDLTLIA STDNASCLPS PLPEGAWVDY
HNYNTPDELV KQFGMFDNVD RSVPYFIGEY SRWEIPWPNM QGSVAEAVFM IGLERNSDVV
KMAAYAPLLQ LVNSTQWTPD LISFTQNPNM VIDSTSYYVQ QMFSVNRGDT IKEVTSDSAF
GPVYWVASSS GSSYYVKLAN YGADTQEVSV SIPGMSSGKL TVLADSDPEA YNSDTQTLVT
PSESNVQASN GQFSFTLPAW SVAVLTAN