ID   ABFB_ASPOR              Reviewed;         506 AA.
AC   Q2UIM2; Q96VA0; Q96VA1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=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=AO090023000001;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION,
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 42149 / RIB 40, and HL15;
RX   PubMed=16233386; DOI=10.1016/s1389-1723(03)80123-8;
RA   Hashimoto T., Nakata Y.;
RT   "Synergistic degradation of arabinoxylan with alpha-L-arabinofuranosidase,
RT   xylanase and beta-xylosidase from soy sauce koji mold, Aspergillus oryzae,
RT   in high salt condition.";
RL   J. Biosci. Bioeng. 95:164-169(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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.
CC       {ECO:0000269|PubMed:16233386}.
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 5.5. Stable between pH 4.0 and 6.5.
CC         {ECO:0000269|PubMed:16233386};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:16233386};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:16233386}.
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; AB073860; BAB71803.1; -; Genomic_DNA.
DR   EMBL; AB073861; BAB71804.1; -; Genomic_DNA.
DR   EMBL; BA000051; BAE58593.1; -; Genomic_DNA.
DR   RefSeq; XP_001820595.1; XM_001820543.1.
DR   AlphaFoldDB; Q2UIM2; -.
DR   SMR; Q2UIM2; -.
DR   STRING; 510516.Q2UIM2; -.
DR   GlyCosmos; Q2UIM2; 1 site, No reported glycans.
DR   EnsemblFungi; BAE58593; BAE58593; AO090023000001.
DR   GeneID; 5993498; -.
DR   KEGG; aor:AO090023000001; -.
DR   VEuPathDB; FungiDB:AO090023000001; -.
DR   HOGENOM; CLU_029332_3_0_1; -.
DR   OMA; WNYPTRY; -.
DR   OrthoDB; 93406at5052; -.
DR   BRENDA; 3.2.1.55; 522.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006564; Chromosome 3.
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   GO; GO:0045490; P:pectin catabolic process; IEA:TreeGrafter.
DR   CDD; cd23399; beta-trefoil_ABD_ABFB; 1.
DR   FunFam; 2.60.120.200:FF:000131; Probable alpha-L-arabinofuranosidase B; 1.
DR   FunFam; 2.80.10.50:FF:000059; Probable alpha-L-arabinofuranosidase B; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.80.10.50; -; 1.
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; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR   PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   SUPFAM; SSF110221; AbfB domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   1: Evidence at protein level;
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="Alpha-L-arabinofuranosidase B"
FT                   /id="PRO_0000394607"
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         473
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        91
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"
FT   CONFLICT        46
FT                   /note="T -> A (in Ref. 1; BAB71804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="I -> T (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="K -> E (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="S -> T (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="T -> K (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="R -> K (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        410
FT                   /note="L -> F (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="L -> H (in Ref. 1; BAB71803)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  52195 MW;  A0D6B300C19C9420 CRC64;
     MSSGLSLERA CAVALGIVAS ASLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGALYQV
     KRGSDGSTTD IAPLSAGGVA DAAIQDSFCA NTTCLITIIY DQSGRGNHLT QAPPGGFNGP
     ESNGYDNLAS AVGAPVTLNG KKAYGVFMSP GTGYRNNAAS GTATGDKAEG MYAVLDGTHY
     NSACCFDYGN AEVSNTDTGN GHMEAIYYGD NTVWGSGAGS GPWIMADLEN GLFSGLSSTN
     NAGDPSISYR FVTAVVKGEA NQWSIRGANA ASGSLSTYYS GARPSASGYN PMSKEGAIIL
     GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQADIVAAK YAIASLTSGP ALTVGSSISL
     QVTTAGYTTR YLAHDGSTVN TQVVSSSSTT ALRQQASWTV RTGLANSACL SFESVDTPGS
     YIRHYNFALL LNANDGTKQF YEDATFCPQA GLNGQGNSIR SWSYPTRYFR HYENVLYVAS
     NGGVQTFDAT TSFNDDVSWV VSTGFA
//