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Database: UniProt
Entry: H1YER4_9SPHI
LinkDB: H1YER4_9SPHI
Original site: H1YER4_9SPHI 
ID   H1YER4_9SPHI            Unreviewed;      1201 AA.
AC   H1YER4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Glycoside hydrolase family 2 sugar binding {ECO:0000313|EMBL:EHQ30824.1};
GN   ORFNames=Mucpa_6775 {ECO:0000313|EMBL:EHQ30824.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ30824.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ30824.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ30824.1,
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; EHQ30824.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1YER4; -.
DR   STRING; 714943.Mucpa_6775; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_271141_0_0_10; -.
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; 2.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   InterPro; IPR021720; Malectin_dom.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 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   Pfam; PF11721; Malectin; 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; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHQ30824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002774}.
FT   DOMAIN          76..213
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          222..326
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          339..473
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          647..704
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          739..905
FT                   /note="Malectin"
FT                   /evidence="ECO:0000259|Pfam:PF11721"
SQ   SEQUENCE   1201 AA;  134188 MW;  319973C938048CDA CRC64;
     MSKYIVPGMQ CRSSGYLTLM GKCLLLWVFV LGPFHVLSQS HIRQDISLSS GWLTIASDSD
     QNAYAGFENP EFNTKNWKQV NVPHTWNNYE GYRRLKHGDR HGYAWYRTSF TVNCVSAGKV
     YFLYFEGVAS YATVWLNGKQ VGYHAGGRTT FTLDVSKYLL SGKPNLLAVR ADHPDHIQDL
     PWVCGGSSDE VGFSEGSQPM GIFRPVHLIV TNPVRIQPFG VHIWNDTTVT EKAARLNIET
     EVKSYSNKER KVTVISRLVN RDGIVVGEVS SDAILPGGAT SIYKQMLNLT HVRLWSLQDP
     YLYSVVSKVI DAQRLTDQES TPYGIRWISW PIGRSDNRKV FLLNGKPVFI NGVAEYEHLM
     GNSHAFTKEQ VKTRVMQVKS AGFNAFRDAH QPHNLEYQKY WDELGILWWP QFTAHIWYNT
     PQFKENFKIL LADWVKERRN NPANVLWGLQ NESKLPAEFA AECSSIIRQL DPTASSQRKI
     TTCNGGAGTD WDVPQNWTGT YGGDPLTYAA DVQKQVLIGE YGAWRSIDLH TEGPFVPSGA
     LSEDRLDQMM ETKIRLAESV KNKTAGQFQW LLSSHENPGR VQGGEGLREL DRVGPVNYKG
     LLTAWGEPTD AFYLYRANYS PKDKEPMVYI VSHTWPNRWL SPGTRDSICV YSNCDEVELF
     NDVDDVSLGK KTNGGIGTHF QWDRVNIQYN VLYAVGYVKG KIVARDFIIL NHLPQAPNFA
     SLLQGNKNLL KPQSGLKYLY RVNCGGPDYR DQFGNLWLAD VHQTNNKTWG SSSWTDDFAG
     MPAMFGSQRR IFDLIRGTND SPLFQTFRYG LNKLKYDFPL PDGDYELELY FTEPWYGTGG
     GMDCTGWRLF DVAVNDQVII HNLDIWHEAG HDEALKKTVK VHITDGHLAL SFPRVQSGQA
     IISAIAVASA NQNVQAAAAS ASLINNLVVT DPSQAKNWYL KSWLDIGDKP YDNDETEISD
     LPPNLYGAEW IKVPKVTNQQ GDLLAKFSLS ADADVYIGIN EAVKQIPAWM HDYDFTKTFV
     QTDANGGSKF NIYHKRFKVG SQVNLGSSAD KAPMYFIAVV PVSQMEPATD LKPTTAYKAE
     LATIAGDDVV RGDVAGKKAV TFKTPSGSSI TWPISTGVAD VHELRIKYLN TTEKQLTAEI
     TVLAADGTVM KAGTMKFGPT TADKWKTVST TTGTSINAGN YKVVLKAVDA QGLSISGLEV
     Q
//
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