MA26A_ASPNC
ID MA26A_ASPNC Reviewed; 335 AA.
AC A2R6F5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase man26A {ECO:0000303|PubMed:21632240};
DE EC=3.2.1.78 {ECO:0000269|PubMed:21632240};
DE AltName: Full=Endo-(1,4)-beta-mannanase man26A {ECO:0000305};
DE Flags: Precursor;
GN Name=man26A {ECO:0000303|PubMed:21632240}; ORFNames=An15g07760;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21632240; DOI=10.1016/j.biortech.2011.04.070;
RA Zhao W., Zheng J., Zhou H.B.;
RT "A thermotolerant and cold-active mannan endo-1,4-beta-mannosidase from
RT Aspergillus niger CBS 513.88: Constitutive overexpression and high-density
RT fermentation in Pichia pastoris.";
RL Bioresour. Technol. 102:7538-7547(2011).
CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans.
CC {ECO:0000269|PubMed:21632240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000269|PubMed:21632240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26.5 mg/ml for locust bean gum {ECO:0000269|PubMed:21632240};
CC KM=2.87 mg/ml for guar gum {ECO:0000269|PubMed:21632240};
CC KM=23.5 mg/ml for konjac glucomannan {ECO:0000269|PubMed:21632240};
CC Vmax=5000 umol/min/mg enzyme toward locust bean gum
CC {ECO:0000269|PubMed:21632240};
CC Vmax=769.2 umol/min/mg enzyme toward guar gum
CC {ECO:0000269|PubMed:21632240};
CC Vmax=1250 umol/min/mg enzyme toward konjac glucomannan
CC {ECO:0000269|PubMed:21632240};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:21632240};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:21632240};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21632240}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR EMBL; AM270352; CAK42663.1; -; Genomic_DNA.
DR RefSeq; XP_001397297.1; XM_001397260.1.
DR AlphaFoldDB; A2R6F5; -.
DR SMR; A2R6F5; -.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR CLAE; MAN26A_ASPNG; -.
DR PaxDb; A2R6F5; -.
DR EnsemblFungi; CAK42663; CAK42663; An15g07760.
DR GeneID; 4988377; -.
DR KEGG; ang:ANI_1_1806134; -.
DR VEuPathDB; FungiDB:An15g07760; -.
DR HOGENOM; CLU_016930_2_0_1; -.
DR BRENDA; 3.2.1.78; 518.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR40079; PTHR40079; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51764; GH26; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..335
FT /note="Mannan endo-1,4-beta-mannosidase man26A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000221105"
FT DOMAIN 32..331
FT /note="GH26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT ACT_SITE 279
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 335 AA; 37700 MW; 2CA82230D417CA4E CRC64;
MFAKLSLLSL LFSSAALGAS NQTLSYGNID KSATPEARAL LKYIQLQYGS HYISGQQDID
SWNWVEKNIG VAPAILGSDF TYYSPSAVAH GGKSHAVEDV IQHAGRNGIN ALVWHWYAPT
CLLDTAKEPW YKGFYTEATC FNVSEAVNDH GNGTNYKLLL RDIDAIAAQI KRLDQAKVPI
LFRPLHEPEG GWFWWGAQGP APFKKLWDIL YDRITRYHNL HNMVWVCNTA DPAWYPGNDK
CDIATIDHYP AVGDHGVAAD QYKKLQTVTN NERVLAMAEV GPIPDPDKQA RENVNWAYWM
VWSGDFIEDG KQNPNQFLHK VYNDTRVVAL NWEGA
