ID   KSBGL_SPHMU             Reviewed;         422 AA.
AC   Q9ZG90;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Keratan-sulfate endo-1,4-beta-galactosidase {ECO:0000303|PubMed:9831650};
DE            EC=3.2.1.103 {ECO:0000269|PubMed:3096984, ECO:0000269|PubMed:9831650};
DE   AltName: Full=Endo-beta-galactosidase {ECO:0000303|PubMed:3096984};
DE   Flags: Precursor;
OS   Sphingobacterium multivorum.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=28454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-65; 108-126;
RP   128-131; 133-152; 157-164; 176-183 AND 185-203, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=9831650; DOI=10.1016/s0378-1119(98)00496-x;
RA   Leng L., Zhu A., Zhang Z., Hurst R., Goldstein J.;
RT   "Cloning, functional expression and purification of endo-beta-galactosidase
RT   from Flavobacterium keratolyticus.";
RL   Gene 222:187-194(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3096984; DOI=10.1093/oxfordjournals.jbchem.a121770;
RA   Ito M., Hirabayashi Y., Yamagata T.;
RT   "Substrate specificity of endo-beta-galactosidases from Flavobacterium
RT   keratolyticus and Escherichia freundii is different from that of
RT   Pseudomonas sp.";
RL   J. Biochem. 100:773-780(1986).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Hydrolyzes internal endo-beta-galactosyl linkages in keratan
CC       sulfate and in various neolacto-type glycosphingolipids, producing
CC       sulfated and non-sulfated disaccharides, and glucosylceramides
CC       respectivly. {ECO:0000269|PubMed:3096984, ECO:0000269|PubMed:9831650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-galactosidic linkages in
CC         keratan sulfate.; EC=3.2.1.103; Evidence={ECO:0000269|PubMed:3096984,
CC         ECO:0000269|PubMed:9831650};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9831650}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; AF083896; AAD04036.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZG90; -.
DR   SMR; Q9ZG90; -.
DR   CAZy; CBM16; Carbohydrate-Binding Module Family 16.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033930; F:keratan-sulfate endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..46
FT                   /evidence="ECO:0000269|PubMed:9831650"
FT   CHAIN           47..422
FT                   /note="Keratan-sulfate endo-1,4-beta-galactosidase"
FT                   /id="PRO_0000430729"
FT   DOMAIN          47..292
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   DOMAIN          291..406
FT                   /note="CBM-cenC"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ   SEQUENCE   422 AA;  45783 MW;  E072456A740D14AC CRC64;
     MRKTKFWLVL SLIATSLSIF ACKKDSTATK NPIPEVSKAK ASTKLLNATT VATTDYELIW
     SDEFNSSGGF DSTKWSYADR GTVAWNKYMT SLPAYASQDG SNLVLRMDNA VVAGDPVAYH
     AGGVKSMGKF SMTYGKVEVR AKFTQGRGSW PAIWMMPEPA TAYGGWPSCG EIDSMEHVNN
     ESVMYHTIHN GSVTNANGGS TASKSATYNT TDYNLYTMIW SPNDIRFYVN NSLQYTYARV
     SGGGTQQWPF DVPFYLILNQ AGGAGWPGAI TNADLPFSMQ VDYVRVYKLP LFSNGDFESG
     VIYPWTTWGG GSSVVSTDAR TGTKCIRETG GETSIEQYLT GLTPNTTYRF GGYAKVSAAG
     QSVSIGVKNY GGTAVDATIG TTSYSNNSVT FTTGANNTTA TVYFYKPLSG TVYGDDFYLE
     KL