ABNA_ASPFU
ID ABNA_ASPFU Reviewed; 321 AA.
AC Q4WYX7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase A;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase A;
DE Short=ABN A;
DE Flags: Precursor;
GN Name=abnA; ORFNames=AFUA_3G14620;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; AAHF01000002; EAL92126.1; -; Genomic_DNA.
DR RefSeq; XP_754164.1; XM_749071.1.
DR AlphaFoldDB; Q4WYX7; -.
DR SMR; Q4WYX7; -.
DR STRING; 746128.CADAFUBP00003385; -.
DR EnsemblFungi; EAL92126; EAL92126; AFUA_3G14620.
DR GeneID; 3512291; -.
DR KEGG; afm:AFUA_3G14620; -.
DR VEuPathDB; FungiDB:Afu3g14620; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR InParanoid; Q4WYX7; -.
DR OMA; GHLWAPD; -.
DR OrthoDB; 796026at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..321
FT /note="Probable arabinan endo-1,5-alpha-L-arabinosidase A"
FT /id="PRO_0000394620"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT SITE 149
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000250|UniProtKB:P94522"
SQ SEQUENCE 321 AA; 34036 MW; 9D9BFFE699F10574 CRC64;
MSASVFVVVA SCLAALAHGY ANPGSCLGAC NVHDPALIRR ESDGKYFRFS TGNKISYASS
SSIEGPWTVL GSVLPSGSSI DLPGNDDLWA PDVSLVNGVY HVYYSVSTFG SQSSAIGLAT
SSTMDLNSWT DHGSTGIQSS SSKPYNAIDG NLFKDGGTYY MNFGSFWHDI YQAPMNSAAT
SVASSSYNIA YNPSGTHAVE GAFMYKYGNY YYLFFSAGIC CGYDTSRPAS GEEYKIKVCR
STSATGNFVD ANGVACTNGG GTVVLESHGN VYGPGGQGVF TDPSLGPILY YHYVDTTIGY
ADSQKLFGWN KIDFSSGWPV V
