ABFA_ASPKW
ID ABFA_ASPKW Reviewed; 628 AA.
AC Q8NK90; G7XYQ0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=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=AKAW_10173;
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-43 AND 482-494,
RP SUBCELLULAR LOCATION, INDUCTION, FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=NBRC 4308;
RX PubMed=16233515; DOI=10.1016/s1389-1723(03)80187-1;
RA Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I.,
RA Matsuzawa H.;
RT "Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and
RT characteristics of the encoding genes from shochu koji molds, Aspergillus
RT kawachii and Aspergillus awamori.";
RL J. Biosci. Bioeng. 96:232-241(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 4308;
RX PubMed=22045919; DOI=10.1128/ec.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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.
CC {ECO:0000269|PubMed:16233515}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. Stable between pH 3.0 and 7.0.
CC {ECO:0000269|PubMed:16233515};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:16233515};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233515}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR EMBL; AB085903; BAB96815.1; -; Genomic_DNA.
DR EMBL; DF126487; GAA92059.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NK90; -.
DR SMR; Q8NK90; -.
DR STRING; 40384.Q8NK90; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR VEuPathDB; FungiDB:AKAW_10173; -.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR InParanoid; Q8NK90; -.
DR SABIO-RK; Q8NK90; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:UniProtKB.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019566; P:arabinose metabolic process; IDA: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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:16233515"
FT CHAIN 26..628
FT /note="Alpha-L-arabinofuranosidase A"
FT /id="PRO_0000394598"
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 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 140
FT /note="D -> E (in Ref. 1; BAB96815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 67959 MW; 162C5F34386D5705 CRC64;
MVAFSALSGV SALSLLLCLV QHAHGVSLKV STQGGNSSSP ILYGFMFEDI NHSGDGGIYG
QLLQNPGLQG TTPNLTAWAA VGDATIAIDG DSPLTSAIPS TIKLDVADDA TGAVGLTNEG
YWGIPVDGSE FQSSFWIKGD YSGDITVRLV GNYTGTEYGS ATITHTSTAD NFTQASVKFP
TTKAPDGNVL YELTVDGSVA AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLADMKGSFL
RFPGGNNLEG NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP
VLGVWDGFAL ESGGNTPITG DALTPYIDDV LNELEYILGD TSTTYGAWRA ANGQEEPWNL
TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA STSEADCLPE SMPEGSWVDY
HDYSTPDGLV GQFNYFDNLD RSVPYFIGEY SRWEIDWPNM KGSVSEAVFM IGFERNSDVV
KMAAYAPLLQ LVNSTQWTPD LIGYTQSPDD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF
GPLYWVASSA GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADNDPDA YNSDTQTLVT
PSESTVQASN GTFTFSLPAW AVAVLAAN
