ID A0A150VJF7_9PEZI Unreviewed; 946 AA.
AC A0A150VJF7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=M433DRAFT_56759 {ECO:0000313|EMBL:KYG50679.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG50679.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG50679.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG50679.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG50679.1}.
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; JPDO01000001; KYG50679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VJF7; -.
DR STRING; 766039.A0A150VJF7; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000075602; 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; 1.
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, ECO:0000313|EMBL:KYG50679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..946
FT /note="Beta-mannosidase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571654"
FT DOMAIN 279..350
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 754..838
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 860..943
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 946 AA; 105740 MW; 62BD1F6F839CC999 CRC64;
MRTALPLLAA NLSLLSEAQR IINLSGRDWT LTGSDGNVSS VPAQVPSQQY LDLQAAGVVG
NTLYGDNDVN QIWVEKSNWT YMSGSLSTLK SGNASQTYLV FEGLDTFASI SFCNESIGTT
NNQFRQYIFD ITSILSSCEG EPRLAIDFGS ASTITQTLGH QANITGNNAQ DNIAGPGNWA
ATCSPDSLYS CRIWARKEQN DFGWDWSPSL APAGPWLPIY AIQLNDQNPT YINNALVDIY
RQGQMPNLSP DQGKPWVFNV SLDCTGTIPY GAGLRLTLKD ATTHKTVLQT NLENVNSSIE
TITGSTIVNQ SSVDLWWPVG MGDQKLYSAS IDIVHDGNCI ASVERRVGFR TIVLNLSRIS
AEQVAQGLLP GANWNFEVNG HVFYAKGSNF VPPSPFWPSV NQTHMQQLFN LVTEGNQNML
RVWSSGAYLP DWIYHMADEM GILLWSEFEF SDAVYPNTSE YLANYEAEAY YQVRRVNYHP
SLALWAGGNE LETMILGGYP DGNSTFFLEQ YRQIQEELLI KCVYANSHSI SYIPSSTYNG
YLSLNFSSVE PQLPRYDNKS SPEALYLDSD YYNYDASIAF NLSTYPIGRF ADEFGFISMP
SLPSWQDVAP PADLYMESPT VIHHNRHFGS DLPANATIAE QSLAGIEQMT TAVKMWYPTP
NLSDSVANFS AWIYSTQVFQ ASFYQHQIAV YRRGSGLPNR QLGSLYWQLE DLWVAPTWAS
IESNNRQKIL YYTAKDIYSP VIVYAYYNIS NYDLQVWVTS DLWEAVRGTV EYEWIDWSGK
KLSVLSNGTS GSTSAAFTVG PINSTQVLNW PSAKEILRSG GLNTSDAILR VNISATGEER
HQQYTHEYYF HPAALNEVPL QDPNLLLTHT GCSGCVDFTV TAQDAVAAWV WLEIPTNAVL
GYWSDNGFWM NKGESRTVRF KVWKDWTAGK WVDTVTVRSM WNNTLS
//
