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Database: UniProt
Entry: W4UZM3_9BACE
LinkDB: W4UZM3_9BACE
Original site: W4UZM3_9BACE 
ID   W4UZM3_9BACE            Unreviewed;       800 AA.
AC   W4UZM3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN   ORFNames=JCM10512_4385 {ECO:0000313|EMBL:GAE85914.1};
OS   Bacteroides reticulotermitis JCM 10512.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE85914.1, ECO:0000313|Proteomes:UP000019131};
RN   [1] {ECO:0000313|EMBL:GAE85914.1, ECO:0000313|Proteomes:UP000019131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE85914.1,
RC   ECO:0000313|Proteomes:UP000019131};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT   Isolated from the Gut of a Termite.";
RL   Genome Announc. 2:e00072-14(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE85914.1}.
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DR   EMBL; BAIV01000033; GAE85914.1; -; Genomic_DNA.
DR   RefSeq; WP_044164966.1; NZ_BAIV01000033.1.
DR   AlphaFoldDB; W4UZM3; -.
DR   STRING; 1445607.JCM10512_4385; -.
DR   OrthoDB; 3308423at2; -.
DR   Proteomes; UP000019131; 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; -; 1.
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   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   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:UP000019131};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..800
FT                   /note="F5/8 type C domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004851637"
FT   DOMAIN          317..456
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   ACT_SITE        40
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            149
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   800 AA;  89772 MW;  31187EFDB20980C3 CRC64;
     MNRLYFWLAA LLCGTVSVLA QASFDTPGTG NPVIPGYFAD PTVKKFGDTY YIYATTDGSG
     AGFGPAQVWT SKDFANWTLM PMNWPDSHWI WAPDVMRHSD GKYYYFYCQP CIIHCGVSDT
     PRGPWKNILG ESEAVLIPDR FVTNAITLDG QTFVDDDGSV YMYWGTWGIY KGFGCGAGKM
     TSDLKGFSKT RLIPNTEATD FFEAPFVIKR NGIYYFMYSS GSCHDQTYRV QYATSDAPLG
     PYKYGGCILE TSADGTIHGP GHHSILQEGD NYYIVYHRHD NPHANRGFHR QVCIDRMTFD
     AEGNIQKIIP THDGVGALAP STVQSKNLAY QKTVRASSFY DDNFRPELAV DDNNGTLWRP
     RGMGQEWIEI DLGSNQQIQT IWTQFQYGTQ FYQYLIETSV NGKQWSVFAD KRNNHLAGSP
     MVDFGKTKAR YVRLTFTGGQ KNGFGGAIWN IKVFGGIEAS APQQWLGLTA ADWNGREWEN
     NEGMLGGSFK LKQGAARTQR IAGRDALVLE PGTTLEFLHP LLSPSTEHTL SVLVYRLGKW
     QSDEVKSSLS NGKILLQSGA EPLIITNLRY YNWVQEEAEK AFDATMDIVR LPAANLQKKG
     LVVSITADAF SLGDTVQYIP NNGVKGIFEG IKAPSIVEET AGKKGFRFDG SQVFRSNFQL
     PTTLLDNAPY TLEAWVLNPT IDLNECVADF TTSHDELEKI MLVNGTEPRC GVINHYGWYE
     DAGYKNLNEW AGKWQHIYIC FDGRIEQVYV NDQLVSEKDI QLLIKPSQFV TLGLNAEGNW
     PFTGYLHSLK LWDEYLPKLK
//
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