MAND_EMENI
ID MAND_EMENI Reviewed; 381 AA.
AC Q5AVP1; C8VBY8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase D;
DE EC=3.2.1.78;
DE AltName: Full=Endo-beta-1,4-mannanase D;
DE Flags: Precursor;
GN Name=manD; ORFNames=AN7639;
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 5 (cellulase A) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000130; EAA61825.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF79796.1; -; Genomic_DNA.
DR RefSeq; XP_680908.1; XM_675816.1.
DR AlphaFoldDB; Q5AVP1; -.
DR SMR; Q5AVP1; -.
DR STRING; 162425.CADANIAP00000757; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblFungi; CBF79796; CBF79796; ANIA_07639.
DR EnsemblFungi; EAA61825; EAA61825; AN7639.2.
DR GeneID; 2869716; -.
DR KEGG; ani:AN7639.2; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_4_1_1; -.
DR InParanoid; Q5AVP1; -.
DR OMA; LFWQYGQ; -.
DR OrthoDB; 1003648at2759; -.
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; IBA:GO_Central.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; PTHR31451; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 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..381
FT /note="Mannan endo-1,4-beta-mannosidase D"
FT /id="PRO_0000393711"
FT ACT_SITE 192
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 299
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 381 AA; 41603 MW; 2D1871678CF69515 CRC64;
MKHLLSLVCT LGAATLAASA AAEAGSMPSA NGLDFVIDGE ASYFAGSNAY WLSFLTNNAD
VDLALDHFAE SGLKILRIWG FSDVTAEPSD NKVYFQLHQN GSSTVNTGPN GLERLDYIIS
GAEKRGIKLV IPLVNYWDDF GGMNAYISAY GGDKPGWYTN DKIQAAYHAY VKAVVSRYVD
SPAIFAWELA NEPRCSGCDT SIINQWATKT SSFIKSLDPN HMVAMGDEGM GLPGDSNYPY
SYYEGNDFAL NLAIPDIDFG TLHLYTTDWG VSNNSWGNKW VQDHAAVCKS AGKPCLFEEY
GMKGNHCTYE LAWQKTALAT PGMAADLFWQ FGENLSSGQT HNDKYTVYYG SNEWKCVVSD
HVAAVAVRRY RLPVGGGQHG P
