ABFB_ASPAW
ID ABFB_ASPAW Reviewed; 499 AA.
AC Q9C4B1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
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;
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 18-27.
RC STRAIN=ATCC 38854 / NBRC 4033;
RX PubMed=16233515; DOI=10.1016/s1389-1723(03)80187-1;
RA Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I.,
RA Matsuzawa H.;
RT "Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and
RT characteristics of the encoding genes from shochu koji molds, Aspergillus
RT kawachii and Aspergillus awamori.";
RL J. Biosci. Bioeng. 96:232-241(2003).
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}.
CC -!- CAUTION: Lacks the conserved Asp residue in position 297 essential for
CC alpha-L-arabinofuranosidase activity. Its enzyme activity is therefore
CC unsure. {ECO:0000305}.
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DR EMBL; AB046701; BAB21567.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C4B1; -.
DR SMR; Q9C4B1; -.
DR CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
DR CLAE; ABF54B_ASPAW; -.
DR UniPathway; UPA00667; -.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..499
FT /note="Probable alpha-L-arabinofuranosidase B"
FT /id="PRO_0000394602"
FT REGION 18..335
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 336..499
FT /note="ABD"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT SITE 176..177
FT /note="Cis-peptide bond"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..31
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 81..86
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 176..177
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 401..439
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ SEQUENCE 499 AA; 52646 MW; 839695CA1D57629F CRC64;
MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT
TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDTDGYDNL
ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE ATGTATGDEA EGMYAVLDGT HYNDACCFDY
GNAETSSTDT GAGHMEAIYL GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS
YRFVTAAVKG GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGYNSN
GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV SLRVTTPGYT
TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE
LLLNANDGTK QFHEDATFCP QAALNGEGTS LRSWSYPTRY FRHYENVLYA ASNGGVQTFD
SKTSFNNDVS FEIETAFAS
