ID   ABNB_NEOFI              Reviewed;         372 AA.
AC   A1DHW8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 76.
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=NFIA_089320;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW18975.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; DS027696; EAW18975.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_001260872.1; XM_001260871.1.
DR   AlphaFoldDB; A1DHW8; -.
DR   SMR; A1DHW8; -.
DR   STRING; 36630.CADNFIAP00008113; -.
DR   GeneID; 4587430; -.
DR   KEGG; nfi:NFIA_089320; -.
DR   eggNOG; ENOG502S2VU; Eukaryota.
DR   OrthoDB; 796026at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006702; 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..372
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase B"
FT                   /id="PRO_0000394631"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        59
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        252
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            179
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        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  41116 MW;  B1E2FB8A6B1D2C54 CRC64;
     MAVLVALFCL VTWALCTRIP QYSTQGTQQL QQPEKTPHPH PRPEDPFPPT HAADFKIHDP
     SIIHVDGTYY SYSVGKHIRI HQAPSLDGPW KRTGTVLDAD SVIPKGDRKA PWAPQTVHHG
     DTYYCFYAVS NSGCRDSAIG VATSKSPGPG GWTDHGLLVQ SGTGKGSDEH PFASSNTIDP
     SVFVGEDGHG YLMFGSFWSG IWQVPLDETL LSVAGDTRSE ARQLVYMEKA PLPASKHPNP
     LCREPSGARP IEGSFLSYHE PWYYLWFSYG KCCKFDTKNL PPPGREYSIR VGRSKSPRGP
     FVDKQGRDLA NGGGEIVYAS NRDVYAPGGQ AVLTEKSGDI LYYHYCRYPA VQETEVDADL
     TVNKSTSYDF WV