ID A0A0F6A3G8_9GAMM Unreviewed; 813 AA.
AC A0A0F6A3G8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=RN22_01940 {ECO:0000313|EMBL:KKD62102.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD62102.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD62102.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD62102.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-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:KKD62102.1}.
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DR EMBL; LASY01000008; KKD62102.1; -; Genomic_DNA.
DR RefSeq; WP_046302880.1; NZ_LASY01000008.1.
DR AlphaFoldDB; A0A0F6A3G8; -.
DR PATRIC; fig|1581149.3.peg.4460; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
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; 2.
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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 194..291
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 648..723
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 735..811
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 813 AA; 92745 MW; 95C997DE575394B5 CRC64;
MTQLILDGEW TLTSLTDDSI VAPIKIPGDV HSALLVADKI PDPYYGCNET DVQWVSEHDW
LLTKSFEVDS PTLEAPRIDL MLSMVDTMAS VAVNGEVVLL CANMFREYRV DVRPYLQQGE
NILTVTLKRA DIEAKARAER LPFPVPWAVG NNQIPHMNTL RKTQCHAGWD WGVCLLASGI
YDSVKLQPIH NVALKGVRTA QQWQSNGQCD LTVSIDAETV GTDSAAIECV LTSPCGESQS
TTISADAESL ACGFTIAHPE RWWPAGYGSQ PLYSLTVSVE GQHITKRIGL RELHLDTTPD
EVGSAMTFVV NGKAIMSKGA NWIPLDAMPG LQTPDRYRQL LEDAKAANMN MIRVWGGGMY
ERDCFYELCD ELGLMVWQDL MFACALYPST PEFLKDVEQE VAYQVRRLSD HSSIALWCGD
NEVIGAIGWY PESRTNREKY VVNYDRLNRV LQEVVEREDP YRRFWASSPC NGELDFGDAW
HDDNKGDMHF WDVWHSGKSF DAYHTVKPRF CSEFGYQSWP SLPTVKTFAS EDDWNVTSPT
FEQHQKNGRG NSIMTEMFTR YFRFPKDFAQ MLYLSQVQQA LAIKTASEYW RANKPLCRGI
LYWQLNDCWP VSSWSSIEYT GRWKQLHYHA KRFFDVKAAV FVEEQDALAL RLINDEHRNV
DAKGQVTWYD WQGEVIDTWP FETKLGEDDN QTVWQCDRQV IDERKHQGFF HVVMECDGKE
ITNTWFDDVY KRLPLPKASV DVEIMEGRDG LQLVLKSDLP AFFVHLEFEG EGRFSDSSFT
LMPCSPVTVN FEGCADVEAM KAGLRVYQLS ETF
//