ID A0A087QR20_APTFO Unreviewed; 822 AA.
AC A0A087QR20;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN ORFNames=AS27_15586 {ECO:0000313|EMBL:KFM03674.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03674.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM03674.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03674.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL225822; KFM03674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QR20; -.
DR STRING; 9233.A0A087QR20; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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:UP000053286};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 286..424
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 645..738
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 742..820
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM03674.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KFM03674.1"
SQ SEQUENCE 822 AA; 94606 MW; 011C87F0B6FD030F CRC64;
DPYYRFNDVM YRWISLDNWT YSRTFKTPFD VRKWQKVNLV FEGVDTVAQI LINNITLGRT
DNMFNRYSFD ITSVIKEVNF IEVRFLSAIS YAAEQSRCHK AYSIPPACPP PVQKGECHAN
FIRKEQCSFS WDWGPSFPTQ GIWKDVRIEA YNHYHLIHFS LTSFFVKSAW QWSLEIESIF
DVVSSKPIAG LVTVSIPKLQ TQQTFSVKLQ PGEGSIVLLV NINKVRSSTV EAWWPNGHGK
QTGYNMTTTF IMEAGYQIEK FSKAYFRTVE LVEESIPGSP GLSFYFRING RPIFIKGSNW
IPADSFQDRV TYDILWLLLK SAADANMNAL RVWGGGVYEQ DEFYDICDEL GIMIWQDFMF
ACALYPTDQN YLESVRAEVS HQVRRLKSHP SIILWSGNNE NEAAIASNWF SIPYADREVY
IKDYVMLYVK NIREIVLTED KSRPFIASSP TNGLESVKEG WLSQNPYDTH YGDTHFYDYS
NDCWNWTVYP KTRFASEYGF QSWPSFSTIE KVSSTEDWSY TSNFSLHRQH HENGNDQMLQ
QIGHHFKLPQ STDPIKKFKD MIYLTQVMQA QCIKTETEFY RFSQSEIIKG EGHTMGALYW
QLNDIWQAPS WASLEYGGKW KLLHYFAQNF FAPLLPVAYE DKGVLYIYGV SDLHVDHKLT
LRVVVHTWSS LEPVCTLAKD GVTVKAQSAV PIYKESINDL LERCRNCTRK SCVITFCLVG
EGGLQSPTNH HFLSSLKDAV GLEKTQLSAS VSQRDDTYVF VLQTTAIAPF VSLDVGNIKG
RFSDNGFLMT EKKKVVVFYP WEPTSVEELE KSLALTSLVD VV
//
