ID   ABNC_ASPTN              Reviewed;         320 AA.
AC   Q0CRJ6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase C;
DE            EC=3.2.1.99;
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase C;
DE            Short=ABN C;
DE   Flags: Precursor;
GN   Name=abnC; ORFNames=ATEG_03688;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476598; EAU35490.1; -; Genomic_DNA.
DR   RefSeq; XP_001212866.1; XM_001212866.1.
DR   AlphaFoldDB; Q0CRJ6; -.
DR   SMR; Q0CRJ6; -.
DR   EnsemblFungi; EAU35490; EAU35490; ATEG_03688.
DR   GeneID; 4318802; -.
DR   VEuPathDB; FungiDB:ATEG_03688; -.
DR   eggNOG; ENOG502QTQG; Eukaryota.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   OMA; AAFMFER; -.
DR   OrthoDB; 796026at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..320
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase C"
FT                   /id="PRO_0000394637"
FT   ACT_SITE        31
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            148
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"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   320 AA;  35390 MW;  6C6F1BE35B83F382 CRC64;
     MYRSTLLFLF IALVNAFANP GPCTGDCWTH DPGLYQRKSD GRYFRFATGG GIHISSAPAI
     VGPWEDNGFA LPNGSKINHA GNDNLWAPDV HYQENTKKYY MYYSVSVLGK KDSVIGVASS
     DTMEVGSWTD HGSIGLNTSN NPPYNTIDAN WIRIDGAPAL NFGSYWQGIF QVPLKNPFEL
     AEIAPHQIAW NASLNHRIEA AFEFKHGNYY YLTFSSGLGG NYDVNLPAQG EEYSIHVCRS
     EGGRNNFVDK SGRSCRESGG TTLLASHGNV YAPGGQGIVE DKNLGQVLYY HYADKTKGLA
     KTDYQFGWNR LNWVDGWPSV