ID F3MCM2_9BACL Unreviewed; 506 AA.
AC F3MCM2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EGG34907.1};
GN ORFNames=HMPREF9412_4162 {ECO:0000313|EMBL:EGG34907.1};
OS Paenibacillus sp. HGF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG34907.1, ECO:0000313|Proteomes:UP000004272};
RN [1] {ECO:0000313|EMBL:EGG34907.1, ECO:0000313|Proteomes:UP000004272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG34907.1,
RC ECO:0000313|Proteomes:UP000004272};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EGG34907.1}.
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DR EMBL; AEXS01000119; EGG34907.1; -; Genomic_DNA.
DR AlphaFoldDB; F3MCM2; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000004272; 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:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 307..499
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 16
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 122
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 506 AA; 56308 MW; A012093F64B20C07 CRC64;
MEMTYQNPVI SGFHPDPSVC RVGGDYYLVT SSFGYYPGVP LFHSNDLVHW TQIGHCLTRK
EQLDLRNAGT STGIYAPTIR FYQGMFYMTT TNVSGGGNFY VTSEDPSGAW SDPVFVDHPG
IDPDLFFDED GTVYYTTSWN QGIYQSRIDI ETGQKLSEVR LLWNGTGGQY PEAPHLYRVG
AWYYLLISEG GTEYGHMVTV ARSKRPEGPF ESCPHNPILT HRSLLKPIQA TGHADLVQAP
DGSWWAVFLG IRPVGYPQRH HLGRETFLAP VSWTGDGWPV IGENGVVHET MPSGNLRLQR
VTSPPVRDDF VDSELAPYWN FLRSPHPDHG SLTEKESCLT LNGSAATLND GAAAFLGRRQ
QHFNMKASVH LTFAPQQDGE EAGLTVFMNE RFHYELAVIR IDGCRKMIFR RRIGSLWKVE
SEAPWSSDSV VLTIQADKEK YAFGFAGGGQ EPCWFGEGEC AMLATEVAGG FTGVLIAMYA
TGNGVRSVSP AHFDWFDYQA LEDVVL
//
