ABFB_ASPCL
ID ABFB_ASPCL Reviewed; 506 AA.
AC A1CGD1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=ACLA_066470;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027053; EAW11011.1; -; Genomic_DNA.
DR RefSeq; XP_001272437.1; XM_001272436.1.
DR AlphaFoldDB; A1CGD1; -.
DR SMR; A1CGD1; -.
DR STRING; 5057.CADACLAP00006216; -.
DR EnsemblFungi; EAW11011; EAW11011; ACLA_066470.
DR GeneID; 4704554; -.
DR KEGG; act:ACLA_066470; -.
DR VEuPathDB; FungiDB:ACLA_066470; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR OMA; HYNGACC; -.
DR OrthoDB; 783026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006701; 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_0000394603"
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 426
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 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; 51886 MW; CDEB3D1906F35DD2 CRC64;
MLSQPSRERA FVLALGLVVS SSLAAAAPCD IYSSGGTPCV AAHSTTRALY SAYSGPLYQV
KRGSDGATTN IAPRSAGGVA NAAAQDTFCA SMTCLITVIY DQSGRGNHLT QAPPGGFKGP
EANGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAS GTAIGDAAEG MYAVLDGTHY
NGGCCFDYGN AETSSLDTGN GHMEAIYFGT NTVWGSGSGS GPWIMADLEN GLFSGSSPAN
NAGDPSVSYR FLTAAIKGGP NRWAIRGANA ASGSLATYYS GARPNASGYN PMSKEGAIIL
GIGGDNSNGA QGTFYEGVMT SGYPSDATEN AVQADIVAAN YAVTSLTSGP ALTVGSAISL
RATTSCCTTR YLAHTGSTIN TQVVSSASAT TLKQQATWTV RTGLANSGCF SFESKDTPGS
FIRHSNFALV LNGNDGTKQF KEDATFCPQA GLNGQGSSIR SWSFPTRYFR HYSNVLYAAS
NGGVHTFDAA GSFNDDVSWV ISSGFA
