MANE_EMENI
ID MANE_EMENI Reviewed; 355 AA.
AC Q5AWB7; C8VCC9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable mannan endo-1,4-beta-mannosidase E;
DE EC=3.2.1.78;
DE AltName: Full=Endo-beta-1,4-mannanase E;
DE Flags: Precursor;
GN Name=manE; ORFNames=AN7413;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR EMBL; AACD01000128; EAA61784.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF78427.1; -; Genomic_DNA.
DR RefSeq; XP_680682.1; XM_675590.1.
DR AlphaFoldDB; Q5AWB7; -.
DR SMR; Q5AWB7; -.
DR STRING; 162425.CADANIAP00000012; -.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR EnsemblFungi; CBF78427; CBF78427; ANIA_07413.
DR EnsemblFungi; EAA61784; EAA61784; AN7413.2.
DR GeneID; 2869806; -.
DR KEGG; ani:AN7413.2; -.
DR VEuPathDB; FungiDB:AN7413; -.
DR eggNOG; ENOG502QT55; Eukaryota.
DR HOGENOM; CLU_016930_2_0_1; -.
DR InParanoid; Q5AWB7; -.
DR OMA; AWWLWFM; -.
DR OrthoDB; 792920at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; IPR016714; MANB/E.
DR PANTHER; PTHR40079; PTHR40079; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PIRSF; PIRSF018168; Mannan-1_4-beta-mannosidase; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51764; GH26; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..355
FT /note="Probable mannan endo-1,4-beta-mannosidase E"
FT /id="PRO_0000395077"
FT DOMAIN 35..348
FT /note="GH26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT ACT_SITE 296
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 355 AA; 39620 MW; 37816EA753D5E877 CRC64;
MKFSQLILPF SAALSLVGSG VATPTTKPVN PRASRPARNL LAHLVRSAGN GTTLSGQQEL
KDADWVTDNV GFSPVILGVD LMDYSPSRVE FGAVSTSIED AITYATQGGI ITICWHWGEL
SHDWMTDERL TTLLTLGSPS GTYNTTEQPW WSNFYTEATS FNLSAAMNPA SRDYKLILRD
IDAIAEQLAR LKDIPVLFRP LHEAEGGWFW WGATGAEPCK ALYRLLFDRL TKKHGLNNLL
WVWNSKDPLW YPGNEYVDVV SVDVYADNGD HSSQLEAYQA LQGLTGNFSK LIALGEVGNI
PDPELMREDG AQWAYWVTWN GDFIRGETKN PMEFKKAVYA SELVYTLDEI QGWNL