ID A0A0M2XWK9_9SPHI Unreviewed; 516 AA.
AC A0A0M2XWK9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KKO90024.1};
GN ORFNames=AAW12_19400 {ECO:0000313|EMBL:KKO90024.1};
OS Sphingobacterium sp. Ag1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO90024.1, ECO:0000313|Proteomes:UP000034524};
RN [1] {ECO:0000313|EMBL:KKO90024.1, ECO:0000313|Proteomes:UP000034524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO90024.1,
RC ECO:0000313|Proteomes:UP000034524};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKO90024.1}.
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DR EMBL; LBGU01000043; KKO90024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2XWK9; -.
DR PATRIC; fig|1643451.3.peg.4529; -.
DR Proteomes; UP000034524; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..516
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005647527"
FT DOMAIN 320..512
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 33
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 144
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 516 AA; 57399 MW; 9D230A64525D89BF CRC64;
MKISAFVFSS MITFLGATAQ QAHNPIIFAD VPDMSMIRVG DTYYMSSTTM HMNPGVPIMK
SKDLVNWTMI NYAYDRLGDQ DELNLSNHKN AYGHGSWASS LRFHEGRYYV STFSANTGKT
HVYQTADIEH GPWTSKEFQP MMHDHSLFFD EGKIYMIWGG GRIYIAELSP DFSGVKAGTQ
RVLIENASLP ANPKEGKAGL PAEGSQMFKI NGMYYLFNIS WPAGGMRTVI VHRASQLEGP
YEGKVVLQDQ GVAQGGLIDM PNGKWYAYLF QDYGAVGRIP FLVPVNWEDG WPVLGIDGKV
PTTLDLAANK SLSPGIVSSD DFERKAGEPA LPLVWQWNHN PAVDLWSVTE RSGFLRLRTG
DLTEDFLSAK NTLTQRTIGP SCSAAIAVEV SNMKDGDFAG LSLLQKNYGL VGVRMEGNTK
SLVMINAMTG APQELAKIDL KQQRVFFKAS CDFSNKKDTA QFFYSTDGHN WNRIGNVLKM
SYTIPHFMGY RFGLFNYASK AAGGYVDFDY FHLTSN
//
