ABFB_ASPKW
ID ABFB_ASPKW Reviewed; 499 AA.
AC Q8NK89; G7XUM7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=AKAW_08685;
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-27 AND 421-432,
RP SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND BIOTECHNOLOGY.
RC STRAIN=NBRC 4308;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 4308;
RX PubMed=22045919; DOI=10.1128/ec.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 19-499 IN COMPLEX WITH SUBSTRATE,
RP DOMAIN, ACTIVE SITE, DISULFIDE BONDS, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, GLYCOSYLATION AT ASN-202, AND MUTAGENESIS OF 176-CYS-CYS-177;
RP THR-204; GLU-221 AND ASP-297.
RC STRAIN=NBRC 4308;
RX PubMed=15292273; DOI=10.1074/jbc.m405390200;
RA Miyanaga A., Koseki T., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.;
RT "Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a
RT novel carbohydrate-binding module that can bind arabinose.";
RL J. Biol. Chem. 279:44907-44914(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-499 OF THE ALA-221 MUTANT IN
RP COMPLEX WITH SUBSTRATE.
RC STRAIN=NBRC 4308;
RX PubMed=16846393; DOI=10.1042/bj20060567;
RA Miyanaga A., Koseki T., Miwa Y., Mese Y., Nakamura S., Kuno A.,
RA Hirabayashi J., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.;
RT "The family 42 carbohydrate-binding module of family 54 alpha-L-
RT arabinofuranosidase specifically binds the arabinofuranose side chain of
RT hemicellulose.";
RL Biochem. J. 399:503-511(2006).
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:15292273, ECO:0000269|PubMed:16233515}.
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 Kinetic parameters:
CC KM=0.76 mM for L-arabinofuranose {ECO:0000269|PubMed:15292273,
CC ECO:0000269|PubMed:16233515};
CC pH dependence:
CC Optimum pH is 4.0. Stable between pH 3.0 and 7.0.
CC {ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16233515};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:15292273, ECO:0000269|PubMed:16233515};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expressed in the presence of L-arabitol and L-arabinose, and
CC repressed in the presence of sucrose and glucose.
CC {ECO:0000269|PubMed:16233515}.
CC -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC a C-terminal arabinose-binding domain (ABD).
CC {ECO:0000269|PubMed:15292273}.
CC -!- BIOTECHNOLOGY: Contribute to an increase in cereal utilization and
CC formation of aroma in shochu brewing. {ECO:0000269|PubMed:16233515}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR EMBL; AB085904; BAB96816.1; -; Genomic_DNA.
DR EMBL; DF126474; GAA90571.1; -; Genomic_DNA.
DR PDB; 1WD3; X-ray; 1.75 A; A=19-499.
DR PDB; 1WD4; X-ray; 2.07 A; A=19-499.
DR PDB; 2D43; X-ray; 2.80 A; A=19-499.
DR PDB; 2D44; X-ray; 2.30 A; A=19-499.
DR PDB; 6SXR; X-ray; 1.64 A; A=19-499.
DR PDB; 6SXS; X-ray; 1.86 A; AAA=19-499.
DR PDB; 6SXT; X-ray; 1.47 A; A=19-499.
DR PDBsum; 1WD3; -.
DR PDBsum; 1WD4; -.
DR PDBsum; 2D43; -.
DR PDBsum; 2D44; -.
DR PDBsum; 6SXR; -.
DR PDBsum; 6SXS; -.
DR PDBsum; 6SXT; -.
DR AlphaFoldDB; Q8NK89; -.
DR SMR; Q8NK89; -.
DR STRING; 40384.Q8NK89; -.
DR CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
DR CLAE; ABF54B_ASPKA; -.
DR iPTMnet; Q8NK89; -.
DR VEuPathDB; FungiDB:AKAW_08685; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR InParanoid; Q8NK89; -.
DR BRENDA; 3.2.1.55; 514.
DR SABIO-RK; Q8NK89; -.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; Q8NK89; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
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 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..499
FT /note="Alpha-L-arabinofuranosidase B"
FT /id="PRO_0000394606"
FT REGION 18..335
FT /note="Catalytic"
FT REGION 336..499
FT /note="ABD"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15292273"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:15292273"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292273,
FT ECO:0000269|PubMed:16846393"
FT SITE 176..177
FT /note="Cis-peptide bond"
FT /evidence="ECO:0000269|PubMed:15292273"
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:0000269|PubMed:15292273"
FT DISULFID 21..31
FT /evidence="ECO:0000269|PubMed:15292273"
FT DISULFID 81..86
FT /evidence="ECO:0000269|PubMed:15292273"
FT DISULFID 176..177
FT /evidence="ECO:0000269|PubMed:15292273"
FT DISULFID 401..439
FT /evidence="ECO:0000269|PubMed:15292273"
FT MUTAGEN 176..177
FT /note="CC->AA: Decreases the affinity toward the
FT substrate."
FT /evidence="ECO:0000269|PubMed:15292273"
FT MUTAGEN 204
FT /note="T->A: Reduces thermostability and catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15292273"
FT MUTAGEN 221
FT /note="E->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15292273"
FT MUTAGEN 297
FT /note="D->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15292273"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6SXT"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6SXT"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6SXT"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2D43"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1WD3"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2D44"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6SXR"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 430..435
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 446..456
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6SXT"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:6SXT"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:6SXT"
SQ SEQUENCE 499 AA; 52598 MW; 94B340130BB18746 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 ILGIGGDNSN
GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV SLRVTTPGYT
TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE
LLLNANDGTK QFHEDATFCP QAALNGEGTS LRSWSYPTRY FRHYENVLYA ASNGGVQTFD
SKTSFNNDVS FEIETAFAS
