ID H1YBQ2_9SPHI Unreviewed; 801 AA.
AC H1YBQ2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Glycoside hydrolase family 2 sugar binding {ECO:0000313|EMBL:EHQ26015.1};
GN ORFNames=Mucpa_1866 {ECO:0000313|EMBL:EHQ26015.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ26015.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ26015.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ26015.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) 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; CM001403; EHQ26015.1; -; Genomic_DNA.
DR AlphaFoldDB; H1YBQ2; -.
DR STRING; 714943.Mucpa_1866; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_0_1_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000002774; Chromosome.
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; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
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 Pfam; PF02837; Glyco_hydro_2_N; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHQ26015.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..801
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003558538"
FT DOMAIN 30..176
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 190..293
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 301..462
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 621..679
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 693..794
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 801 AA; 90176 MW; CFC9F8508B4E9737 CRC64;
MKSVLTLLFL SLTAMVSAQN VLTGSRKQLF DYDWKFSLAQ ERTASQPDFN DTKWRTINLP
HDWSIEGQTK ADNPSGNDGG YFPAGTGWYR KKFLIPTAMK GKKISVYFEG VYMNSEVFIN
GKSLGVRPYG YSAFVYDITP YLNYNGDNIL VVKADNSRQK NSRWYSGSGI YRHVWVTVTD
AVHIGNWGTV ITTNNISKAS AEVEIKTILK NELPTPQNIS LYAVLTAKNK RQAGNTVIQV
ALAPNETKEF IQNVVIKDPL LWSPNHPDLY KVRISVKRGF KIIDETFNDF GIRSLAFSTE
NGFQLNGKKI ILNGGCAHHD NGILGAAAYD RAEEKKVELL KAAGFNAVRT SHNPPSEAFL
NACDRLGLLV IDESFDGWRQ SKTAYDYTMY FDTWWQRDVE TMVLRDRSHP SIFMWSIGNE
VIERKKPEAI ATATMMAKFI KTLDTTRPIT SAMTTWDSEW EMFDPLFAAY DIAGYNYQLY
RAADDHKRIP SRIIVQTESY PKDAFDNWKL SHENSYILGD FVWTAIDYLG ESSIGRYFYP
GDPTGQHYEK PLFPWHGAYC GDIDLTGWRK PISHYRELLY SDKEELYLAV KEPNPASGPI
SLTSWAVWPT WESWTWPGFE GKDIQVEVYS KYPAVRLYLN DKLLGEQLTA EEQQFKATFT
IPYTPGVIKA VAVKDGKEVE TRILKTAGKA AGIKLIADRR ALSANAQDLS YVTVEIVDEN
GRPVPDANNQ LSFNISGEGT IAGLGNANLQ DTDPYIGNQH KAWKGRALAI LKSTQKPGKL
ALQVSSPGLK TASLIMNTIS R
//
