ID A0A1T4ZWI3_9SPHI Unreviewed; 1179 AA.
AC A0A1T4ZWI3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=F5/8 type C domain-containing protein {ECO:0000313|EMBL:SKB26829.1};
GN ORFNames=SAMN05660226_00178 {ECO:0000313|EMBL:SKB26829.1};
OS Parapedobacter luteus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623280 {ECO:0000313|EMBL:SKB26829.1, ECO:0000313|Proteomes:UP000190541};
RN [1] {ECO:0000313|EMBL:SKB26829.1, ECO:0000313|Proteomes:UP000190541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22899 {ECO:0000313|EMBL:SKB26829.1,
RC ECO:0000313|Proteomes:UP000190541};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; FUYS01000001; SKB26829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4ZWI3; -.
DR STRING; 623280.SAMN05660226_00178; -.
DR Proteomes; UP000190541; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18608; GH43_F5-8_typeC-like; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000190541};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1179
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011984348"
FT DOMAIN 333..469
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 157
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 1179 AA; 130251 MW; 43D02E7F4738E8BB CRC64;
MYRDCSLLLS VFLRFFCFNV FLSSANGQAL APHERPSMGN PIIPGYFADP TVRKIGDTYY
IYATTDGNGW GAGPSQVWTS KDFVNWTIQP MNWPNTHWYW APEMTPGYDG RYYLYYSQPV
QLYGAVSDSP VGPWSPLQPE GEALVPNYKI PGVITLDGQA FRDDDGKIYL YWGTWGIYPD
HGCAVGLLNP DMKTFADIKL IPNTDATDFF EAPFVFKRKG IYYFMYSSGR CEDDTYRVQY
AMSKHGPMGP FVYPEAHNPV LSTNSDGTVH GPGHHSILQE GDQYYIIYHR HNNPHSGGGF
HRQVAADRME FDHEGNIVKV VPTHGGVGYL GENTIPYKNL AFGAKVTASS AYSEAFSPQF
AVDDNNGTLW KAADNQASAW LQLDLGEVKA VRTIHTQFEY ATWYYGYVIE YSADGATWQT
FSNRRDNRRW GSPMIDEGDV RARYLRMTID QTQVPGMFKA IWNIKVFAEA GVGRPVLSDE
QPLTPRDTPG GLLIDVDAAK LPLGSMLTKL PNNGSLAGEW NAEGAPYVAM LAGRQAVIFD
GKTAFRSSFA VPTTLSGNSS HTVSAWVFNP TVERHEPLLA WTQGAQDLSR GIVGYGHDRG
NGAVVRGAWP DVAYQTVPEA GQWHHIAVTF DGYMERLYVD GTEVNTSNKM LLMNAARAFM
MGKAFGESDY FSGALSSLKV YDRALSAAEV IADYQHENTS KALVWLRADE LAFGAVSRWE
NEGVLGGDLQ VASGTLKASI ICGRIAAAAE RPVTIQAAPV AEAFGQKQDQ DATLMVDFCI
TGKKSALYGI SGIGHQLNIG QWGQLVVMRK DGLAHVYVND QPVKVQQDQL NRYFVDIETG
LFSLNDMAVA SIRVFEGAWT NEQLAANGYQ EMQVGTCAWG AAVFEVPPMF INENTVFMRA
EAIDGVGMQY QFVDSIGNVC SGWLDRTDFL VVCDNADRIP AFQVVAKDRY GYVTKPTNPI
QAGTRAVASP ADFAVSHDFL DDGVVGTHWD GISGDRDAFQ TVSSGGGELQ LSSVNTQWNG
SRSTGPFLYR EVSGDFVAQT ELDDVSGRDE RRGSPNETGI MLSFEGTDGR QHLLQSSVMT
GWNVGNLVTV IDGRGRRQQN NGRGWSFHRH LQLQRLGSTI YLRSSEDGRN WQELPGSPYH
MDSLVGNKPV HVGLYQVTNE NKQGYGTFKS FTVFKSQTD
//
