ABNC_ASPCL
ID ABNC_ASPCL Reviewed; 319 AA.
AC A1CN18;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=ACLA_098980;
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; DS027058; EAW08955.1; -; Genomic_DNA.
DR RefSeq; XP_001270381.1; XM_001270380.1.
DR AlphaFoldDB; A1CN18; -.
DR SMR; A1CN18; -.
DR STRING; 5057.CADACLAP00009119; -.
DR EnsemblFungi; EAW08955; EAW08955; ACLA_098980.
DR GeneID; 4702439; -.
DR KEGG; act:ACLA_098980; -.
DR VEuPathDB; FungiDB:ACLA_098980; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_009397_5_0_1; -.
DR OMA; AAFMFER; -.
DR OrthoDB; 796026at2759; -.
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 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..319
FT /note="Probable arabinan endo-1,5-alpha-L-arabinosidase C"
FT /id="PRO_0000394632"
FT ACT_SITE 31
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P94522"
FT SITE 146
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 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 319 AA; 34929 MW; 1A3F2F287AF566A0 CRC64;
MFVYTLIFLF LAAANAYSNP GPCSGNCWTH DPGLYQRKSD GKYFLFATGG GIHISSADDL
AGPWTDDGFV LPDGSSIDLD GQNNLWAPDL HYRDGTYYLY YSVSALGSQN SAIGVATSET
LEAGSWTDHG STGVTSTPNS PYNTIDGNWI AVGDKQYLNF GSYWQNLFQV ELADGLKVKE
GATPHQLSYN ASGIHRQEAA FMFERNSYFY LTFSGGVALG YNATWPAQGE EYHINVCRST
SATGGFVDKN GVSCLNSGGS LLLASHGFVY GPGGQGILED RNKELVLYYH YADTRIGKAV
EDYQFGWNQL KWENDWPSV
