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Database: UniProt/TrEMBL
Entry: Q01U55_SOLUE
LinkDB: Q01U55_SOLUE
Original site: Q01U55_SOLUE 
ID   Q01U55_SOLUE            Unreviewed;       835 AA.
AC   Q01U55;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Glycoside hydrolase family 2, sugar binding {ECO:0000313|EMBL:ABJ86815.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Acid_5873 {ECO:0000313|EMBL:ABJ86815.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ86815.1};
RN   [1] {ECO:0000313|EMBL:ABJ86815.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ86815.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP000473; ABJ86815.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01U55; -.
DR   STRING; 234267.Acid_5873; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   KEGG; sus:Acid_5873; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_5_0_0; -.
DR   InParanoid; Q01U55; -.
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; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABJ86815.1}.
FT   DOMAIN          213..317
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          323..516
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          662..720
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          754..829
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   835 AA;  92926 MW;  73A777529971894E CRC64;
     MVSDMNLRKS PASGLTRREL FQAASAVIAG AALTSTSSAA TGAPTVRRLT TGWEHYRGGL
     GGVWEVWRGK AASDNVAWDT VAIPHCFNAF DAVDPDHAYY EGPGWYRTSF MPQNPFPNGR
     ILLHFEGAGQ KSEVFVGLER AGAHVGGYDE FTIDITDAAA RAAKRPDAKG QVQLAVLCDN
     SRNPEMIPSD LSDFNRYGGL YRHVNLAYAP AISIEHVQID STTVAGKSDV SVKARLYNPG
     GLKDAVQVEI TVTDAAGKAV HTSTKSLPAW TGEQELASFP VANPALWSPK TPNLYRCSVT
     VKSPHGEQQV EDRFGLRWFE FPKKGLFHLN GEKLFLRGTQ RHEDHAGLAA ALTDDLIRQE
     FHLAKEMGCN FIRLGHYQGS RLALQMADEL GLVVWEEIPW CRGGVGGEQY REQARRMLRN
     MIDQHRNHPS VIFWGLGNEN DWPGDFEVFD EKAVRAFMSE LNEIAHKADP SRMTAIRRCP
     FAADVPDVYS PSIWAGWYSG RYTEYKASTE KEAKKIDRML HIEWGGDSHA RRHSEDPDTV
     IAKISTGQGV EEKDRAYLLT GGTTRASKDG DWSETYICNL FDWHLKEQET MDFLPGSAMW
     VFKDFSTPLR PENPVPRMNQ KGVVERDMTP KEGYYVFQSY WAEKPMARIY GHTWPIRWGA
     AGEQKMVKVY SNCASAELFL NGKSCGVKQR NSQDFPCAGL RWMVPFQAGE NHLRVVAAKG
     AVKVADETRF RYQIEKWDKP AKFVLEETGR EGAVVTLQAR LLDAKGVQCL DARTAVRFAI
     AGDGELLQNL GTSTGSRQVE LYNGRAIIRA RLKPGEAAVT VSAEKLPTAL LTVKT
//
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