ID G1NFQ1_MELGA Unreviewed; 811 AA.
AC G1NFQ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
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 Name=MANBA {ECO:0000313|Ensembl:ENSMGAP00000011854.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000011854.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000011854.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000011854.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|ARBA:ARBA00004740}.
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 AlphaFoldDB; G1NFQ1; -.
DR Ensembl; ENSMGAT00000012736.2; ENSMGAP00000011854.2; ENSMGAG00000011325.2.
DR GeneTree; ENSGT00390000001670; -.
DR InParanoid; G1NFQ1; -.
DR TreeFam; TF105723; -.
DR Proteomes; UP000001645; Chromosome 4.
DR Bgee; ENSMGAG00000011325; Expressed in pancreas and 17 other cell types or tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 InterPro; IPR041447; Mannosidase_ig.
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 Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
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 Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 275..437
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 633..727
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 731..810
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 811 AA; 93187 MW; EC0C2F965E2430F9 CRC64;
MYRWISLDNW TYSRTFKTLF DVRKWQKVNL VFEGIDTVAH ILLNNVTLGR TNNMFNRYSF
DITSMIKEVN FIQVHFISAI SYAAEQSRCH KAYSVPPACP PPVQKGECHA NFIRKEQCSF
SWDWGPSFPT QGIWKDVRIE AYNHYNLIYF SLTPFFVSRA QQWSLEIESI FNVASSKPIA
GLATVNIPKL QTQQTYSVKL QPGEGSIVLL VNISKNSTVE AWWPNGHGKQ IGYNMTTTFI
MEGGYQIEKI SKAYFRTVEL VQEPIPGSPG LSFYFKINGQ PIFMKGSNWI PADSFQDRVT
YDTLWLLLKS AADANMNALR IWGGGIYEQD DFYNICDELG IMIWQDFMFA CALYPTDQDY
LESVRAEVSH QVRRLKSHPS VVLWSGNNEN EAAIASNWFS IPHADREVYI KDYVMLYVKN
IREIVLAEDK SRPFVVSSPT NGLESIKEGW LSKNPYDTHY GDTHFYDYSS DCWNWSVYPR
TRFASEYGYQ SWPSFSTLQK VSSAEDWSYT SNFSLHRQHH ENGNDQMLQQ IGYHFKLPLT
TDPIKKFKDM IYLTQVMQAQ CVKTETEFYR SSRSEIVKGE GHTMGALYWQ LNDIWQAPSW
SSLEYGGKWK LLHYFAQNFF SPLLPVAYED NGVLSIYGIS DFHTDHKLTL KVIVNSWNSL
EPVCTLAKDG VTVKAQSAFS IYKESINALL ERCRNCTRKS CVVSFYLTGE DGLQSPMNHH
FLSSLKDAVG LEKTQLSATV SQQDDVYIFD LQTTAIAPFV TLDVGSIKGR FSDNGFLMME
KKKVVIFYPW EPTSVEELEK SFTLTSLMDV A
//
