ABFB_ASPTN
ID ABFB_ASPTN Reviewed; 506 AA.
AC Q0CEE5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable alpha-L-arabinofuranosidase B;
DE Short=ABF B;
DE Short=Arabinosidase B;
DE EC=3.2.1.55;
DE Flags: Precursor;
GN Name=abfB; ORFNames=ATEG_07939;
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. Able to
CC hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-
CC arabinofuranosyl oligosaccharides, but also in polysaccharides
CC containing terminal non-reducing L-arabinofuranoses in side chains,
CC like L-arabinan, arabinogalactan and arabinoxylan (By similarity).
CC {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 -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC a C-terminal arabinose-binding domain (ABD). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR EMBL; CH476604; EAU32201.1; -; Genomic_DNA.
DR RefSeq; XP_001216560.1; XM_001216560.1.
DR AlphaFoldDB; Q0CEE5; -.
DR SMR; Q0CEE5; -.
DR STRING; 341663.Q0CEE5; -.
DR EnsemblFungi; EAU32201; EAU32201; ATEG_07939.
DR GeneID; 4322793; -.
DR VEuPathDB; FungiDB:ATEG_07939; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR OMA; HYNGACC; -.
DR OrthoDB; 783026at2759; -.
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 GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; PTHR39447; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; SSF110221; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..506
FT /note="Probable alpha-L-arabinofuranosidase B"
FT /id="PRO_0000394608"
FT REGION 27..343
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 344..506
FT /note="ABD"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 305
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT SITE 184..185
FT /note="Cis-peptide bond"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..39
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 89..94
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 184..185
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 409..447
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ SEQUENCE 506 AA; 52197 MW; 10913205A0B91DE1 CRC64;
MLLPRGFNRA VVTALGVVGT GTLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGPLYQV
KRGSDGATTN IAPLSAGGVA NAAAQDSFCA GTTCLITIIY DQSGRGNHLT QAPPGGFKGP
EANGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAS GTATGDAPEG MYAVLDGTHY
NGGCCFDYGN AETSSTDTGN GHMEAIYFGD NTVWGSGSGS GPWIMADLEN GLFSGSSTKN
NAGDPSVSYR FLTAIVKGKP NQWAIRGANA ASGSLSTYYN GARPNASGYN PMSKEGAIIL
GIGGDNSIGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YAVAPLTSGP SLTVGSSISL
RATTSCCTTR YLAHNGSTVN TQVVSSSSST ALKQQASWTV RAGLANSACF SFESKDTPGS
FIRHYDFVLQ LSANDGTKQF YEDATFCPQS GLNGQGSSIR SWNYPTRYFR HYNNVLYAAS
NGGVHTFDAT GSFNDDVSWV VSTSFA
