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Database: UniProt
Entry: Q21GU0_SACD2
LinkDB: Q21GU0_SACD2
Original site: Q21GU0_SACD2 
ID   Q21GU0_SACD2            Unreviewed;       877 AA.
AC   Q21GU0;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Inactivated b-glycosidase {ECO:0000313|EMBL:ABD82089.1};
GN   Name=gly16G {ECO:0000313|EMBL:ABD82089.1};
GN   OrderedLocusNames=Sde_2832 {ECO:0000313|EMBL:ABD82089.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD82089.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD82089.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|ARBA:ARBA00006865}.
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DR   EMBL; CP000282; ABD82089.1; -; Genomic_DNA.
DR   RefSeq; WP_011469305.1; NC_007912.1.
DR   AlphaFoldDB; Q21GU0; -.
DR   STRING; 203122.Sde_2832; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   KEGG; sde:Sde_2832; -.
DR   eggNOG; COG2273; Bacteria.
DR   HOGENOM; CLU_327856_0_0_6; -.
DR   OrthoDB; 9800955at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04080; CBM6_cellulase-like; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.3440; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF17963; Big_9; 1.
DR   Pfam; PF03422; CBM_6; 2.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SMART; SM00606; CBD_IV; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS51175; CBM6; 2.
DR   PROSITE; PS51762; GH16_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ABD82089.1};
KW   Hydrolase {ECO:0000313|EMBL:ABD82089.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..877
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004199627"
FT   DOMAIN          84..338
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   DOMAIN          630..751
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          757..876
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   877 AA;  94233 MW;  CCD5E7B60B5B9AC2 CRC64;
     MVKNKLYLAL SIAAATSLTA CGGGGDAADD TVKRNVFAVG DVFKTQEDGD AVEADVSEND
     FGRGLTFALE SGSTTANGEL VFNADGSFTY TPNADFSGKD SFTYVATHTA SGDTASALVT
     INVISDFETI EESGWTLTWS DEFDSLDSMA WDAMNASASE GVLSVSAVEG QTSYVKSTAA
     LGQAGRIEAS IQLPDGKSLY SGFGLMPMAD MFDGKNALMA IESANNKATA GGHWGIGLVN
     GVEINEPTNA VVRAEFHTYA IEWNESLIRW YIDDIHIHTV DTLNTWSYNL SGDTVVADTT
     TKPFSQDLQI MMELTAASSG LPNAMLVDFV KVYECDTSVT DQIESCAFAA DENVDKLASN
     RIESVGEIVT PLFTDELTSL SWHYSDAEEA VTFVTEQESA VPTHRGIVSQ PDVMEPVAEV
     APVDPVEEGE EGYEEYQAYL AYVDYLNYLE TLAFLDTVDP SRERGAVIRY QSDASTWSNF
     SLNTPSLGLV GKDSALQFDM YIDSASTTTE TIEIRMETGW PFLGTVLLNV ADLQLDTWVT
     YNIPVSDFLA NPFITPDWAV GQDWFLGGNG VEGQPLYLDT NSITKAIVVQ LAAPGHLVFD
     NVAITCVSNE SCFQGPLAKQ PIVKAGPAPI IYEAEAYTAV TGEVQTEDTQ DAGGGQNVGY
     IDAGEALEYT IVAPIDGTYK FQYRLASGLE SASEFDVSID DMLIDGQSLP GTGGWQVWTT
     LESGEFDLTA GEHAIVFNFA GGMNFNWFAI VPPPIAIFIE AEDYSSMAGV QLEDTADEGG
     GQNVGYIDAG DFLQYNVEVP ADGTYFIELR VASSGGSDGF TITSNGITTS TIPVADTGGW
     QNWTTQTVEM QLSAGQQTLR FDFIGGAINF NWINVTN
//
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