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Database: UniProt
Entry: A0A0Q5Q693_9FLAO
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ID   A0A0Q5Q693_9FLAO        Unreviewed;       828 AA.
AC   A0A0Q5Q693;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN   ORFNames=ASG01_10705 {ECO:0000313|EMBL:KQR92391.1};
OS   Chryseobacterium sp. Leaf180.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR92391.1, ECO:0000313|Proteomes:UP000051405};
RN   [1] {ECO:0000313|EMBL:KQR92391.1, ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|EMBL:KQR92391.1,
RC   ECO:0000313|Proteomes:UP000051405};
RX   PubMed=26633631; DOI=10.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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 B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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:KQR92391.1}.
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DR   EMBL; LMPJ01000010; KQR92391.1; -; Genomic_DNA.
DR   RefSeq; WP_055863637.1; NZ_LMPJ01000010.1.
DR   AlphaFoldDB; A0A0Q5Q693; -.
DR   STRING; 1736289.ASG01_10705; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000051405; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:SF1; BETA-MANNOSIDASE; 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; 3.
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:UP000051405};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          208..303
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          665..756
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          759..825
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   828 AA;  96646 MW;  3A01D30AF9413509 CRC64;
     MKYYPYLFFL LLFAKGFSQT SERNLSEENW QFKNSKENTW LSAKVPGMVH LDLLANKVIQ
     DPFKDENEKK VQWVESEDWD YQTVFKVSAR ELQNQNCELV FHGLDTFSEI YLNGKLLKKT
     DNMFRTWNIP VKNDLKVGNN TLQIKFKSSV NIGKDLAKKV PFTMPESPRS FVRKAQYQFG
     WDWGPRLVTA GIWKDVKLNF WNLAKLQNVK IEQKSVTNQK AELIIHAEIF AEQNGKYSFL
     ISNEVNNISL KQGLNKISIP YQILNPKLWQ PNGWGKAMTY LLKFSLKKDA QIIDKKDETI
     GLRTIELIQD LDKKGKSFYF KVNGNPMYAK GTNWIPSDSF TPRITKEKYQ KLIKDCKDAN
     MNMIRVWGGG IYEDDEFYKA CDENGILVWQ DFMFAGSFYP SDEDFLNNVK EEVKDQVSRL
     QNHPSIALWC GNNEIDEAIV NWGYQKQFKY SKEDSLQVWK DYRKVFHEVI PNALKENLTS
     EKNIYWPTSP SIGWGHKESL TEGDSHYWGV WWGEFPFEIY SEKVPRFASE YGFQGMPSLE
     AVKSMFSTNP DLNLENPTVK AHEKNARGFD IIKKYMERDY VVPTDFVKYN YVSQLLQARG
     MKIAIEAHRR EKPDNMGTLY WQLNDCWPVI SWSSIDYLGN WKALHYQVKR SFENKVILAE
     EKSETLNFYA VNDALEKFEN ISLEVQTMDF SGKILIKKEL QPAGKDLKDI LKFESLKTSE
     LFANYDKNKI FLKLSLKDVN SKIIAENIYF FSKPKDLKLT KPRISVKKIS PNEIEISTDV
     LAKDVYLMGQ THFSDNFYDL LPNTKRIIRL SAPVSDIKIL SLWDTLNN
//
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