ID ABNC_NEOFI Reviewed; 321 AA.
AC A1DKY5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 81.
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=NFIA_047920;
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}.
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DR EMBL; DS027698; EAW15456.1; -; Genomic_DNA.
DR RefSeq; XP_001257353.1; XM_001257352.1.
DR AlphaFoldDB; A1DKY5; -.
DR SMR; A1DKY5; -.
DR STRING; 331117.A1DKY5; -.
DR GlyCosmos; A1DKY5; 3 sites, No reported glycans.
DR EnsemblFungi; EAW15456; EAW15456; NFIA_047920.
DR GeneID; 4583867; -.
DR KEGG; nfi:NFIA_047920; -.
DR VEuPathDB; FungiDB:NFIA_047920; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR OMA; EDYQFGW; -.
DR OrthoDB; 2655644at2759; -.
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 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:SF7; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE C; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..321
FT /note="Probable arabinan endo-1,5-alpha-L-arabinosidase C"
FT /id="PRO_0000394639"
FT ACT_SITE 33
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 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 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 35018 MW; A78934EA39150149 CRC64;
MYLYTLILLF LASVNVNAYA DPGACSGNCW THDPGLYQRK SDGKYFRFAT GGGIHIASAD
SLEGPWTDDG YVLPNGSIID LNGKNNLWAP DLHYRDGTYY LYYAVSSLGS QNSAIGVATS
KTMEAGSWTD HGTTGIESTP ASPYNAIDAN WIAVGGTQYA NFGSYWNNLF QVEMTNGLKV
KSGATPHQIA YNASGIHRQE AAFMFERNDY FYLTFSGGIA LGYNDTWPAP GEEYFISVCR
STSATGGFVD KNGVSCLNSG GTLLLASHGF VYGPGGQGIL KDSSKGFVLY YHYADTRIGK
AVEDYQFGWN QLKWENDWPS V
//
