ID B6QB13_TALMQ Unreviewed; 953 AA.
AC B6QB13;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=PMAA_064660 {ECO:0000313|EMBL:EEA25354.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25354.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA25354.1; -; Genomic_DNA.
DR RefSeq; XP_002145901.1; XM_002145865.1.
DR AlphaFoldDB; B6QB13; -.
DR STRING; 441960.B6QB13; -.
DR VEuPathDB; FungiDB:PMAA_064660; -.
DR HOGENOM; CLU_005015_3_0_1; -.
DR OrthoDB; 2504097at2759; -.
DR PhylomeDB; B6QB13; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000001294; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..953
FT /note="Beta-mannosidase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845524"
FT DOMAIN 249..337
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 740..824
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 845..924
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 953 AA; 106662 MW; 584A28D71B8BDF76 CRC64;
MLMRKKILLA AGFPLLTLAQ RVIDLSGDNW TVKNEECNLS APASLPSQVH LDLYAAGVIH
TPEQMKLTFA GSPGRTGHIR VIQSRDCMLN DASASWIVFN GLDTFATIEL CGQLVGTANN
QFRQWQFDVS GALKSCKGDP VISIHFRSAP EIANAIANEP GQETWPDGIQ GLFEFDNRWF
IRKEQSDFGW DWGPAFSPTG PWQPAYLVQF KPNDGVYVLN TDIDIHREGQ VNWLPPDQTR
PWVVNASIVY LGSLPKGASL TVEIKDAQNQ TTIASGSLTN VTTSGNSISG ITTVGADVPK
LWWPTSMGDQ NLYYITINVV NNNGKTLATI TKRTGFRTIV LNQTNITHAQ LALGIAPGAN
WHFEINGHEF YAKGSNFIPP DAFWPRVTED RMRRLFNSIV KGNQNMLRVW ASGAYLPNFI
YDIADEVGVL LWSEFQFGDA LYPVDQVFLD NVAAEVAYNV RRVNHHPSLA LWAGGNELES
LELLQVYENY PEEYARYVGE YEKLFISTIF PLVYDNTHSI SYTPTSTGNG YTNIDFSLAV
PMVERYQNVT PGEYYGDSDY YNYNSAEAFD MSHYPVNRFA NEFGFHSMPS LQTWRQAVYD
EDDLQFNSSV ILHRNHHYPP GGLSLNTTLS AKGMGEMTIA VERYYPIPSK TDPIANFSAW
CLATQRFQAD MYKSQIQFYR RGSGHPERQL GSLYWQLEDI WQAPTWAGIE YDGRWKVLHY
VAKNIFEPVI VAPYWNSTTG QLNVTVTSDL WESVSGTVSM TWYDLSGKPL EKNAGIPSSV
AFDVGPLNIT DILITNINDL SISDLKDAVL ILSLSATGHL PNSNVTTRFS HENFFTPVFT
NEAKLVDPGL KLSYDNSTGK FTVEATKAVS LYTWLDYPSG LVGYFDENSF VLVPGQPKEV
GFTAQQGSLS EDVVRHVTVQ SIWDQAEGLK STVVRVREKG LRPLRDARNQ PDA
//
