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
//