ABFA_PENCN
ID ABFA_PENCN Reviewed; 631 AA.
AC U6A629;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Alpha-L-arabinofuranosidase A;
DE Short=ABF A;
DE Short=Arabinosidase A;
DE EC=3.2.1.55;
DE AltName: Full=Arabinoxylan-arabinofuranohydrolase of 70 kDa;
DE Short=AF-70;
DE Flags: Precursor;
GN Name=abfA; Synonyms=Abf51A;
OS Penicillium canescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5083;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SIGNAL SEQUENCE CLEAVAGE SITE, SUBCELLULAR
RP LOCATION, GLYCOSYLATION AT ASN-28; ASN-85; ASN-180; ASN-252 AND ASN-559,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24211368; DOI=10.1016/j.carres.2013.08.026;
RA Gusakov A.V., Sinitsyna O.A., Rozhkova A.M., Sinitsyn A.P.;
RT "N-glycosylation patterns in two alpha-l-arabinofuranosidases from
RT Penicillium canescens belonging to the glycoside hydrolase families 51 and
RT 54.";
RL Carbohydr. Res. 382:71-76(2013).
RN [2]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=14640962; DOI=10.1023/b:biry.0000009134.48246.7e;
RA Sinitsyna O.A., Bukhtoyarov F.E., Gusakov A.V., Okunev O.N.,
RA Bekkarevitch A.O., Vinetsky Y.P., Sinitsyn A.P.;
RT "Isolation and properties of major components of Penicillium canescens
RT extracellular enzyme complex.";
RL Biochemistry (Mosc.) 68:1200-1209(2003).
CC -!- FUNCTION: Secreted alpha-L-arabinofuranosidase that actively hydrolyzes
CC p-NP-alpha-L-arabinofuranoside. Exhibits significant activity against
CC polymeric arabinose-containing substrates such as arabinan and
CC arabinoxylan. Hydrolyzes also low-molecular-weight and polymeric
CC galactoside-containing substrates such as galactan, xyloglycan, and p-
CC NP-beta-D-galactopyranoside. {ECO:0000269|PubMed:14640962}.
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 Evidence={ECO:0000269|PubMed:14640962};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:14640962};
CC Temperature dependence:
CC Optimum temperature is 67 degrees Celsius. 50 perscent maximal
CC activity is exhibited at 75 degrees Celsius. Reaction time was 10
CC min. {ECO:0000269|PubMed:14640962};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14640962,
CC ECO:0000269|PubMed:24211368}.
CC -!- PTM: Residues Asn-28, Asn-85, Asn-180, Asn-252, and Asn-559 are highly
CC mannosylated with up to 7 mannose residues.
CC {ECO:0000269|PubMed:24211368}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR EMBL; KF482902; AHA15411.1; -; mRNA.
DR AlphaFoldDB; U6A629; -.
DR SMR; U6A629; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR iPTMnet; U6A629; -.
DR UniPathway; UPA00667; -.
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; IPR008979; Galactose-bd-like_sf.
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; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:24211368"
FT CHAIN 18..631
FT /note="Alpha-L-arabinofuranosidase A"
FT /id="PRO_0000426723"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24211368"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24211368"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24211368"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24211368"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24211368"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 68553 MW; AB232E78D5CC17ED CRC64;
MLAEYLLLPL LASYASAVTI SVAKSGGNVT TGLQYGAMEE EINHCGEGGL YAELIRNRAF
QGSTTYPSNL DAWSAVGGST LSLQNLSNPL SSALPTSVRI TGKGTSGISN TGFWGIDVRP
QKYSGSFYVK GSYKGSFTAS LQASNGEVFA STQVSSKSVA NDWVQHEFTL TPKKKASSSN
NTFVLTFDAS KASGGSLDFN LISLFPPTWN NRPNGMRRDL MQALQDLGPK FLRFPGGNNL
EGQTIEGRWK WNETIGPLTQ RPGRATTWGY EETSGMGLVE YMEWCDDLGM EPLAVWAGLA
LNGDVVPEAE LDVYVQDALD ELEFLTGSVD TKYGALRAKY GHPKPWTIRY VEVGNEDNLS
SGLSSYKSYR FQAFYDAITK KYPNIQVLAS TIDMTLPGNA GGDYHLYDIP DNFITKFGMF
DSYSDAHPIL LGEIAATEYN NGVGIDWSNT HFSLYPWWLG SVAEAVFLLG AERNADKIIG
TTYAPFLMNL DSYEWSPTMI SFNSNPDDTA KSTSWHVYNN HMTNTLPATS NDTFGPPLLC
HRCETAKTNS HIFKAAVYNS TADVPVSLTF EGVGRGTTAD LTILTAPSDV SMNAVGGANV
VQSQTTKIKA GKQGVFSFKL PNLSVAVLTT N
