ID ABNA_ASPCL Reviewed; 321 AA.
AC A1CLG4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=ACLA_042100;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027056; EAW09988.1; -; Genomic_DNA.
DR RefSeq; XP_001271414.1; XM_001271413.1.
DR AlphaFoldDB; A1CLG4; -.
DR SMR; A1CLG4; -.
DR STRING; 344612.A1CLG4; -.
DR EnsemblFungi; EAW09988; EAW09988; ACLA_042100.
DR GeneID; 4702768; -.
DR KEGG; act:ACLA_042100; -.
DR VEuPathDB; FungiDB:ACLA_042100; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR OMA; GHLWAPD; -.
DR OrthoDB; 2655644at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006701; 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:SF3; ARABINOSIDASE-RELATED; 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; 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_0000394617"
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; 34386 MW; 0F6F4E185E20EBBB CRC64;
MHPSTFVTTI ACLAGLAHGY ANPGSCSGAC NIHDPALIRR QSDGKYFRFS TGNKISYASS
SSIKGPWTVL GSVLPRGSSI NLPGKTDLWA PDISLVNGAY HLYYSVSAFG SQDSAIGLAT
SATMDPNSWT DHGSTGIRSS SSKPYNAIDA NLFHDGGNYY MTFGSFWHDI YQAPMNSAAT
AVSSGPYNIA YNPSGTHAVE GAFMYKFGKY YYLFFSSGIC CGYDTSRPAA GKEYKIRVCR
STSATGHFVD KHGVSCTNGG GTVVLESHGH VYGPGGQGVF TDPALGPVLY YHYVDTRIGY
ADGQKRFGWN KIDFSSGWPV V
//
