ID E9FXK2_DAPPU Unreviewed; 911 AA.
AC E9FXK2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Beta-mannosidase {ECO:0000256|ARBA:ARBA00015707};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Lysosomal beta A mannosidase {ECO:0000256|ARBA:ARBA00032581};
DE AltName: Full=Mannanase {ECO:0000256|ARBA:ARBA00033445};
GN ORFNames=DAPPUDRAFT_311672 {ECO:0000313|EMBL:EFX88257.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX88257.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX88257.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
CC -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC residue from the non-reducing end of all N-linked glycoprotein
CC oligosaccharides. {ECO:0000256|ARBA:ARBA00003150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; GL732526; EFX88257.1; -; Genomic_DNA.
DR AlphaFoldDB; E9FXK2; -.
DR STRING; 6669.E9FXK2; -.
DR EnsemblMetazoa; EFX88257; EFX88257; DAPPUDRAFT_311672.
DR KEGG; dpx:DAPPUDRAFT_311672; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_3_1_1; -.
DR InParanoid; E9FXK2; -.
DR OMA; QFACASY; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..911
FT /note="Beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003236920"
FT DOMAIN 438..581
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 835..908
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 104517 MW; FADAC784BECE86AE CRC64;
MMRRQQLTFP TLVLLVLINN SLGYEIDLST ANGYAWSAAL PNKSIAVPGR VPGSIYTDLD
EAEIFTGGPL LFRFNDLEYR WVSYEDWDYS LTFDVPANVA SYSAVDLVFY GVDTVADIEL
NGSPLGATNN MFIRYKYNIK DFLKTDVSNE LLIRFKSPVK YARDRYDEQA VDYPVLPTCL
DPAYQGECHA NHIRKMQSSF SWDWGPAFPT VGLWHPVKLE AYNTVSIRDW WVGFERDEIQ
QLWKVDMKIH CETPDSGIDH AGTFTVTITD QQQVVQTLKQ ETVLTGDGNR QVSTPVISFV
VPFSQIKPWM PNGWGEQKLY DMKIEYQETG SAEPPVVLDE KIGFRTVDLI EDDLPTGRTY
YFRVNGEPVF LKGSNWIPSA VLPELITEQY LRELLTASKD AHMNAMRIWG GGIYEFSEFY
RIADELGILI WHDMMYACSM YPANEQFLET VSVEIRQQVR RLSHHPSVLI WAGNNENEAA
LRQNWYGTES KFETYKADYI KLYVDTIKRI LNEEDPSRPF TVSSPSNGKK SEEEGYVSLN
PGNPEYGDVH YYNYFDDMWN WETYPKPRMA TEYGFQALPS VHAWTTAANP IGMDEDWHYD
GQLLFTRQHH PGGNNELVLQ VEGQLGKARE TTQEQRFLDM IYLTQMHQAE AIKIESEHYR
RLQYLDFDGL GHCMGSLYWQ LQDIWQGPSW ASIEYGGRWK PLHHFATKFF APLSFMLWVR
DGNVAIYPHD YRSGADMVPG ILLIKLQSWS QINPIVTERI PNVNGNSTIE WQKPLDSWLS
DNGCSRQTCF LTATYQDPET GRHLAPDSYL YPSNFTAVTN LAKANVQVTS VGQVYESSQS
SWTIDVELST DKPAAFVWLD TTTDRKGRFS DNAFLMSTAT KTVSFWSSDP ITDSTEFSNE
LRIAHLAEII R
//
