ABFB_EMENI
ID ABFB_EMENI Reviewed; 510 AA.
AC O74288; C8VN12; Q5BD09;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, 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=AN1571;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=ArgB2, biA1, and MetG1;
RX PubMed=10217508; DOI=10.1099/13500872-145-3-735;
RA Gielkens M., Gonzalez-Candelas L., Sanchez-Torres P.,
RA van de Vondervoort P., de Graaff L., Visser J., Ramon D.;
RT "The abfB gene encoding the major alpha-L-arabinofuranosidase of
RT Aspergillus nidulans: nucleotide sequence, regulation and construction of a
RT disrupted strain.";
RL Microbiology 145:735-741(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(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:10217508, ECO:0000269|PubMed:16844780}.
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 4.8. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217508}.
CC -!- INDUCTION: Expressed in presence of L-arabinol and repressed in
CC presence of glucose and glycerol. Expression is also pH regulated
CC probably through the action of the pacC transcription factor and is
CC higher at acidic pHs. {ECO:0000269|PubMed:10217508}.
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; Y13759; CAA74084.1; -; Genomic_DNA.
DR EMBL; AACD01000025; EAA64278.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85134.1; -; Genomic_DNA.
DR RefSeq; XP_659175.1; XM_654083.1.
DR AlphaFoldDB; O74288; -.
DR SMR; O74288; -.
DR STRING; 162425.CADANIAP00008202; -.
DR CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
DR CLAE; ABF54B_EMENI; -.
DR EnsemblFungi; CBF85134; CBF85134; ANIA_01571.
DR EnsemblFungi; EAA64278; EAA64278; AN1571.2.
DR GeneID; 2875522; -.
DR KEGG; ani:AN1571.2; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR InParanoid; O74288; -.
DR OMA; HYNGACC; -.
DR OrthoDB; 783026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS: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; IDA:UniProtKB.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..510
FT /note="Alpha-L-arabinofuranosidase B"
FT /id="PRO_0000394609"
FT REGION 25..342
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 343..510
FT /note="ABD"
FT /evidence="ECO:0000250"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT SITE 182..183
FT /note="Cis-peptide bond"
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..37
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 87..92
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 182..183
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT DISULFID 412..450
FT /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ SEQUENCE 510 AA; 52942 MW; 54011DA6AD3BFC22 CRC64;
MTMSRSSRSS VLALALATGS LVAAGPCDIY SSGGTPCIAA HSTTRALYSS YNGPLYQVQR
ASDGTTTTIT PLSAGGVADA SAQDAFCENT TCLITIIYDQ SGNGNDLTQA PPGGFNGPDV
GGYDNLAGAI GAPVTLNGKK AYGVFVSPGT GYRNNEAIGT ATGDEPEGMY AVLDGTHYND
GCCFDYGNAE TSSLDTGNGH MEAIYYGTNT AWGYGAGNGP WIMADLENGL FSGQSSDYNA
GDPSISYRFV TAILKGGPNL WALRGGNAAS GSLSTYYNGI RPTDASGYNP MSKEGAIILG
IGGDNSVSAQ GTFYEGAMTD GYPDDATENS VQADIVAAKY ATTSLISGPA LTVGDTVSLK
VTTSGYDTRY IAHTGSTINT QVVSSSSSST LKQQASWTVR TGLASTAAAN GCVSFESVDT
PGSYIRHSNF ALLLNANDGT KLFSEDATFC PQDSFNDDGT NSIRSWNYPT RYWRHYENVL
YVASNGGVNT FDAATAFTDD VSWVVADGFA
