ABNA_ASPNG
ID ABNA_ASPNG Reviewed; 321 AA.
AC P42256;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=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;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-32 AND
RP 125-139.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=7764386; DOI=10.1007/bf00170387;
RA Flipphi M.J.A., Panneman H., van der Veen P., Visser J., de Graaff L.H.;
RT "Molecular cloning, expression and structure of the endo-1,5-alpha-L-
RT arabinase gene of Aspergillus niger.";
RL Appl. Microbiol. Biotechnol. 40:318-326(1993).
CC -!- FUNCTION: Its preferred substrate is linear 1,5-alpha-L-arabinan. The
CC enzyme activity is progressively reduced as 1,5-alpha-chains become
CC shorter or more highly substituted.
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 -!- INDUCTION: By L-araban, arabinogalactan and L-arabitol.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; L23430; AAA32682.1; -; Genomic_DNA.
DR AlphaFoldDB; P42256; -.
DR SMR; P42256; -.
DR STRING; 5061.CADANGAP00007516; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR CLAE; ABN43A_ASPNG; -.
DR VEuPathDB; FungiDB:An09g01190; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1114612; -.
DR VEuPathDB; FungiDB:ATCC64974_6800; -.
DR VEuPathDB; FungiDB:M747DRAFT_282673; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR BioCyc; MetaCyc:MON-16541; -.
DR UniPathway; UPA00667; -.
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 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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:7764386"
FT CHAIN 20..321
FT /note="Arabinan endo-1,5-alpha-L-arabinosidase A"
FT /id="PRO_0000012204"
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"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 34455 MW; 3087D7D0592A0B20 CRC64;
MYQLLSVASV PLLASLVHGY ADPGACSGVC TTHDPGLIRR ESDGTYFLFS TGNKISYVSA
SSIEGPWTSV GSMLPDGSSI DLDGNDDLWA PDVSYVDGLY YVYYAVSTFG SQDSAIGLAT
SETMEYGSWT DHGSTGIASS SAKIYNAIDP NLIYADGTYY INFGSFWDDI YQVPMKSTPT
AAASSSYNLA YDPSGTHAEE GSYMFQYGDY YYLFYSAGIC CGYDTSMPAS GEEYHIKVCR
STSPTGDFVD SDGTACTDGG GTMVLESHGE VYGPGGQGVY DDPNLGPVLY YHYMNTTIGY
ADSDAQFGWN TIDFSSGWPV V
