ID A0A136PXQ3_9ACTN Unreviewed; 811 AA.
AC A0A136PXQ3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN ORFNames=AWW66_04530 {ECO:0000313|EMBL:KXK63205.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK63205.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK63205.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK63205.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KXK63205.1}.
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DR EMBL; LRQV01000008; KXK63205.1; -; Genomic_DNA.
DR RefSeq; WP_067360188.1; NZ_LRQV01000008.1.
DR AlphaFoldDB; A0A136PXQ3; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000070620; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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 PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 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:UP000070620}.
FT DOMAIN 202..293
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
SQ SEQUENCE 811 AA; 90538 MW; 646BA7EA7A3CA204 CRC64;
MTQRTLHDGW TLHAVPGSPV PTALAGREVP ASVPGCVHTD LLTAGLIPDP YLDDNEVGLS
WIGRTDWVYR STVDWTPGGD DRVDLVCAGL DTVATVSVNG TEVGRTENMH RGYRFDVRSL
LRPGDNTVEV RFDSAYRYAA AQRERLGHRP NAYREPFNFI RKMACNFGWD WGPTLVTAGI
WQPIGLHSWS TARLATVRPL VTVADSTGRV TVHVEVERVA EVPLTVRASV AGVDVEASIP
AGARAAVLDL TVADVRRWWP RGYGEPHRYP LTVTLHDPAG TLLDEWSRRI GFRSVRLDTV
PDAHGTPFTL VVNDVPVFAR GVNWIPDDVF PHRVTRDRLA HRFDQAVGAN VNLLRVWGGG
RYESDDFYDL ADDLGLLVQQ DFLFACAAYP EEEPFATEVA AEAAEQVTRL SVHPSLVLWT
GNNENIWGWH DWGWQEQLDD RSWGRGYYLE LLPRIVAELD PTRPYWPGSP WSGREDRHPN
EPAHGSMHIW DVWNTDDYVR YREYVPRFLA EFGYQAPPAY ATLRRALSDD PLAPDSPGMA
HHQKAVDGDL KLQRGLDAHL PAPADFDEWH YLTQLNQARA IALGVEHFRA HRGVCMGTIV
WQLNDCWPVT SWAAIDGDGR RKPLWYALRR AYADRLLTVQ PRDGGLALVA VNETGQPWRA
PATVTRLTLA GAPRAKTSVE LDVPAYGVMT VPLPAELAGP HEPRAELLVA EAGEEVDRAL
WFFAEDKDVT WPRADFDSTV ERFDGGVRIR VTARTVLRDL TLQPDRLHPD ATVDEALLTL
LPGETATFTV HTPVPLEASA LTTRPVLRAV N
//
