ABFB_ASPFU
ID ABFB_ASPFU Reviewed; 506 AA.
AC Q4WL66;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=AFUA_6G14620;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL89298.1; -; Genomic_DNA.
DR RefSeq; XP_751336.1; XM_746243.1.
DR AlphaFoldDB; Q4WL66; -.
DR SMR; Q4WL66; -.
DR STRING; 330879.Q4WL66; -.
DR EnsemblFungi; EAL89298; EAL89298; AFUA_6G14620.
DR GeneID; 3508653; -.
DR KEGG; afm:AFUA_6G14620; -.
DR VEuPathDB; FungiDB:Afu6g14620; -.
DR HOGENOM; CLU_029332_3_0_1; -.
DR InParanoid; Q4WL66; -.
DR OMA; HYNGACC; -.
DR OrthoDB; 783026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000002530; Chromosome 6.
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:0045490; P:pectin catabolic process; IBA:GO_Central.
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_0000394605"
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 240
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; 52548 MW; 7EE4CD1C4B1A3224 CRC64;
MLPQLSIERA SVFALGLIAT GSLVVAGPCD IYSAGGTPCV AAHSTTRALY SSYSGPLYQV
KRGSDGATAD IAPLSAGGVA NAAAQDSFCD GTTCLITIIY DQSGRGNHLT QAPPGGFSGP
ESNGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAS GTATGDAPEG MYAVLDGTHY
NDACCFDYGN AETSSRDTGN GHMEAIYFGD NTIWGTGSGS GPWIMADLEN GLFSGSSPDN
NSGDPSISYR FLTAVVKGKQ NQWAIRGANA ASGSLSTFYN GARPSVSGYN PMSKEGAIIL
GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YATASLTSGP KLTVGSSISL
QATTPGYTTR YIAHSGSTVN TQVVSSSSST TLKQQASWTV RTGLANSDCF SFESRDTPGS
FLRHYNFVLQ LSANDGTKQF HEDATFCPQA GLNGQGNSIR SWNYPTRYFR HYNNVLYAAS
NGGVHTFDAT SSFNNDVSWV ISTGFA
