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Database: UniProt
Entry: N1MVB8_9SPHN
LinkDB: N1MVB8_9SPHN
Original site: N1MVB8_9SPHN 
ID   N1MVB8_9SPHN            Unreviewed;       847 AA.
AC   N1MVB8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Beta-glucosidase-related glycosidases {ECO:0000313|EMBL:CCW19258.1};
GN   ORFNames=EBBID32_36240 {ECO:0000313|EMBL:CCW19258.1};
OS   Sphingobium indicum BiD32.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW19258.1, ECO:0000313|Proteomes:UP000013201};
RN   [1] {ECO:0000313|EMBL:CCW19258.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW19258.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Le V.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW19258.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW19258.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Nielsen J.L., Zhou N.A., Kjeldal H.;
RT   "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:CCW19258.1}.
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DR   EMBL; CAVK010000183; CCW19258.1; -; Genomic_DNA.
DR   RefSeq; WP_006962452.1; NZ_CAVK010000183.1.
DR   AlphaFoldDB; N1MVB8; -.
DR   Proteomes; UP000013201; Unassembled WGS sequence.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCW19258.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013201};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..847
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004108101"
FT   DOMAIN          422..566
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   847 AA;  91631 MW;  4A0CBA4992F308F5 CRC64;
     MSAILCLLAA ATPSVAPDIA AKIAKMTPAQ KAAQLQSSAP ADGPELPAYD YWNEALHGLA
     RNGVATVFPQ AIGLGATWDP DLMERIGTVV STEARAKYNG LPGQDRRRYQ GLTIWSPNIN
     IFRDPRWGRG QETYGEDPLL TGSLAVGYVK GLQGPDLSQP RVIATPKHLV AHSGPEAGRD
     SFNVQSSAYD MEATYLPAFR MALTQGKALS VMCAYNSVHG VPVCASDWLL NQRVRKDWGF
     DGLVVSDCDA IGNINHYQRY RQTNAAASAV AINAGMDLNC GKAYAALDKA LAEGLTSNET
     VDTALARTFV VRKALGDAFG AKSRWDGIDA VDKTRNQALA LEAARKSLVL LQNDGVLPLK
     RGARIAVIGP NADSLDVLEA NYHGTAADPV TPLAALRKRF DVHYAQGSTL AEGVPVVIPE
     TAFATGLKAE FFADPAMTGA AMVTQTHKRI DFDWNRTPPA PGIPSDRYGV RWTGTLMPEG
     AGRHILRIDV PRCFDCNGHD AVRLWIDDQP VIADTGDNSQ VEVRLDFDDA RPRKIRLELS
     HASEDEGIRL TWVAPPLPQR SFAVAQARTA DAVIAFVGLS PAVEGEALQI EVPGFSGGDR
     TDIALPQAQQ QLLEAVKATG KPLVVVLLSG SAVAMQWAKD NANAIIAAWY PGQAGGTAIS
     DLIEGRYAPS GRLPVTFYTR TRDLPAFVDY NMRERTYRYF HGTPLWGFGH GLSYTHFTYD
     RIEAPSEIAA GTTLTVKARL RNSGDRDGEE VAQAYLIPPE KWQRVGDFND PVLRHSMIGF
     QRVILQKGKD RMISFTLDPR ALSTVDRDGL RAVRPGAYRL FIGGGQPGAA SGVEVPFTIS
     GMQELPK
//
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