ID A0A137Q2Z4_9AGAR Unreviewed; 958 AA.
AC A0A137Q2Z4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-mannosidase A {ECO:0000256|ARBA:ARBA00021795};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase A {ECO:0000256|ARBA:ARBA00031061};
GN ORFNames=AN958_04449 {ECO:0000313|EMBL:KXN81560.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN81560.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN81560.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN81560.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase A subfamily. {ECO:0000256|ARBA:ARBA00007483}.
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DR EMBL; KQ963282; KXN81560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q2Z4; -.
DR STRING; 1714833.A0A137Q2Z4; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
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:SF5; BETA-MANNOSIDASE A; 1.
DR Pfam; PF00703; Glyco_hydro_2; 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; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..958
FT /note="Beta-mannosidase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295001"
FT DOMAIN 255..361
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 769..858
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 866..954
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 958 AA; 107081 MW; 62B2F117C49786E6 CRC64;
MLGLRLTLLI LLTSFVGPAF ADVVNLANLK WTLTNSNRTI NVPSTGPPNQ AHIDLLNAGL
ITEPLLGING TIHDFTQRWI VDENWTYTAD ISPFLESNTF KQSKKTLLVF YGIDTIANIT
LAGKPVAWVN NQFRQYVYDV SDILASPQNH ELVVAFESAW TYGLNYEYPG VRQWVRKIAS
DFGWDWGPAF VPTGIYKPAY FVTLSAPSGK QQTIGTPPIS PGVNERIASS PVFIEESSID
IYKLGESFSV APKEDADWVV NVTLGVQSSS DFQSSSLTLA FPELKARKTF NVLPVQALPN
ASSDGTNWLN AVWQIPDFVP KRWYPHNLGT PQLYNLSVTL DLKSRGNTVD SVTFNTRTGF
RTIQLIQSPY TAEQVQNGIT PGDNWHFNIN GKPFYALGTN IIPFDPFYAR TTTDQVRWVL
ESAAKSGQNM LRIWGGGTYQ PSHPSVAGGV YDFYSICDEL GILAWSELIF SDTMYPINDF
LLESIEPEVR QNVRRVNRHP SNAQWAGGNE IEGIVTNAVP LLKNGTHYLN EYVALFQDFL
QPIVSSEARA VPYTDCSTTK GVLSLDPYEL RLSNATPGEI YGNGERYNYD GSVAFDYSTY
PVSRFMNEFG FHSMPSFYSW EEVLLSPSDF SFNSTVVTSR DHHPPAGSLA FPNPNAPQGQ
AQMTSFVELW LPTPIDSSTN PNKTFTQWCY STQVFHNLAM VAQVAWYRHG AGKGENNLGA
LVWQLNDIWQ GISWSSIEYS GRWKVLQYGL TGIFSPVVIY PFWTARNETL EVLVVSDRWE
SVKGQAQLTW YDWNGTMLST EKHEFTVPSL NNSVIVQKTG LEESILPKGR NVMDVWMLLN
LTAEVDGKTV TNEQWFTPTS LANANLQDPK ISLTHTSNLT FKLSAKGGVG AWTWIDHPAG
TIGIFVDAKT GVPTNGFYLI PGQDRTLRFE LNSALSRVKN PDPKDFVVRS LWDNTHIE
//