ABFB_ASPOR
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 03-AUG-2022, entry version 95.
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;
OC Aspergillus subgen. 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; AP007157; BAE58593.1; -; Genomic_DNA.
DR RefSeq; XP_001820595.1; XM_001820543.1.
DR AlphaFoldDB; Q2UIM2; -.
DR SMR; Q2UIM2; -.
DR STRING; 510516.Q2UIM2; -.
DR CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
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; HYNGACC; -.
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: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 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
