(data stored in ACNUC16935 zone)

SWISSPROT: 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   07-JUN-2017, entry version 86.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION,
RP   AND 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
RT   of a 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community 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
RT   enzymes 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
CC       of 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
CC       chains, like L-arabinan, arabinogalactan and arabinoxylan.
CC       {ECO:0000269|PubMed:10217508, ECO:0000269|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing alpha-L-
CC       arabinofuranoside residues in alpha-L-arabinosides.
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
CC       is higher at acidic pHs. {ECO:0000269|PubMed:10217508}.
CC   -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain
CC       and a C-terminal arabinose-binding domain (ABD). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC       {ECO:0000305}.
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   ProteinModelPortal; O74288; -.
DR   SMR; O74288; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH54; Glycoside Hydrolase Family 54.
DR   mycoCLAP; ABF54B_EMENI; -.
DR   PRIDE; O74288; -.
DR   EnsemblFungi; CADANIAT00008202; CADANIAP00008202; CADANIAG00008202.
DR   EnsemblFungi; EAA64278; EAA64278; AN1571.2.
DR   GeneID; 2875522; -.
DR   KEGG; ani:AN1571.2; -.
DR   HOGENOM; HOG000187007; -.
DR   InParanoid; O74288; -.
DR   KO; K20844; -.
DR   OMA; YPTRYFR; -.
DR   OrthoDB; EOG092C3Z3T; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled 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; IPR007934; AbfB_ABD.
DR   InterPro; IPR013320; ConA-like_dom.
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;
DR   PRODOM; O74288.
DR   SWISS-2DPAGE; O74288.
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    510       Alpha-L-arabinofuranosidase B.
FT                                /FTId=PRO_0000394609.
FT   REGION       25    342       Catalytic. {ECO:0000250}.
FT   REGION      343    510       ABD. {ECO:0000250}.
FT   ACT_SITE    227    227       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    304    304       Proton donor. {ECO:0000250}.
FT   BINDING     225    225       Substrate.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     228    228       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     427    427       Substrate.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     429    429       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     430    430       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     446    446       Substrate.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     475    475       Substrate.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     477    477       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     480    480       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   BINDING     500    500       Substrate.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   SITE        182    183       Cis-peptide bond.
FT                                {ECO:0000250|UniProtKB:Q8NK89}.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     37       {ECO:0000250|UniProtKB:Q8NK89}.
FT   DISULFID     87     92       {ECO:0000250|UniProtKB:Q8NK89}.
FT   DISULFID    182    183       {ECO:0000250|UniProtKB:Q8NK89}.
FT   DISULFID    412    450       {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
//

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