ID   ABNB_ASPTN              Reviewed;         364 AA.
AC   Q0CY27;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase B;
DE            EC=3.2.1.99;
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase B;
DE            Short=ABN B;
DE   Flags: Precursor;
GN   Name=abnB; ORFNames=ATEG_01407;
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAU38164.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; CH476595; EAU38164.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001208772.1; XM_001208772.1.
DR   AlphaFoldDB; Q0CY27; -.
DR   SMR; Q0CY27; -.
DR   STRING; 341663.Q0CY27; -.
DR   GlyCosmos; Q0CY27; 1 site, No reported glycans.
DR   EnsemblFungi; EAU38164; EAU38164; ATEG_01407.
DR   GeneID; 4316117; -.
DR   eggNOG; ENOG502S2VU; Eukaryota.
DR   OrthoDB; 2655644at2759; -.
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   CDD; cd18831; GH43_AnAbnA-like; 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   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF4; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE B; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..364
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase B"
FT                   /id="PRO_0000394629"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            169
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        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   364 AA;  39895 MW;  675856B4AA37E495 CRC64;
     MRRIIKILVV VAVLYLAIIF LFANTRRVVP IHRQTPFPPT HPADLKIHDP SILKVGDKYY
     SYSVGPRIVI HEAPTLSGPW KKTGHVLDKD SIIPKGDRKA PWAPTTIEVA GTYYCYYAVS
     QSGCRNSAIG VATSQSPGPG GWTDHGAIIH TGTGPGSDSA PFDRSNAIDA SVILTPDGNG
     YLNFGSYWTG IWQVPLNADL VSISDVSTNA ARHLAYEPHA FSPGGKNPNP LCGDRSGSHP
     IEGAFVSYRA PFYYLWFSWG KCCKYNPKAL PPRGKEYQIR VGRSTHPQGP FVDRQGVDLI
     EGGGEVVYGS NRDVYAPGGQ GVLTDEGTDI LYYHYLNKTV SLDFWEARLG YNPLIYIDGW
     PVAQ
//