ID A0A133Y8W7_9BACT Unreviewed; 546 AA.
AC A0A133Y8W7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:KXB39535.1};
GN ORFNames=HMPREF1870_01917 {ECO:0000313|EMBL:KXB39535.1};
OS Bacteroidales bacterium KA00344.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB39535.1, ECO:0000313|Proteomes:UP000070254};
RN [1] {ECO:0000313|Proteomes:UP000070254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB39535.1}.
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DR EMBL; LSCT01000166; KXB39535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133Y8W7; -.
DR STRING; 1497954.HMPREF1870_01917; -.
DR PATRIC; fig|1497954.3.peg.1951; -.
DR Proteomes; UP000070254; 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; cd09001; GH43_FsAxh1-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:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..546
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007460047"
FT DOMAIN 342..544
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 156
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 546 AA; 61478 MW; FC9D525BF7A0A593 CRC64;
MMLKQILLTL FMALPVAASA QYRSQVWCPD NGDGTYTNPV INADYSDPDV IAVGDDYYMT
ASSFNCIPGL PILHSRDLVN WEIIGHGVRR LVPDSLFSGK PAHGNGVWAP CIRYHDGEFY
IYWGDPDNGV FMVKTKEPAG TWEDPVLVIE GKGMIDTTPL WDDDGRCYLA NGWANSRNRF
ASVITVRELN KEGTKTIGDP VIVFDGNGTE YRTAEGPKFY KRDGWYWVMF PAGGVATGFQ
VAMRSRNPYG PYEYQKVLAQ GTTDINGPHQ GAWIHTSVGE DWFMHFQDKG AYGRVVHLQP
VTWKDNWPVM GRVPKKGYCG EPYTTYRKPK SASSVVMNPV ESDEFNAPML GKQWQWHANY
AQAYGMPTSL GFFRLYTWKS NETLWNTPNL LLQKTPADKF TATAKLKLIG KAENQFGGIV
MMGLDYSALV VKRVGDQFKL QQITCNKADK KGREEVTTLA TLNKTGQDEN DYQFAIHEEI
YLQMKVDHGQ VNFAYAIDGK TFKPVGKTFT MREGKWIGAK IGLVAQEPTG TTNRGWIDVD
WFRISP
//
