ID I3I4I0_9GAMM Unreviewed; 587 AA.
AC I3I4I0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:EIK42965.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:EIK42965.1};
GN ORFNames=O59_004283 {ECO:0000313|EMBL:EIK42965.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK42965.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK42965.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK42965.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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:EIK42965.1}.
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DR EMBL; AICM01000014; EIK42965.1; -; Genomic_DNA.
DR AlphaFoldDB; I3I4I0; -.
DR STRING; 1134474.O59_004283; -.
DR PATRIC; fig|1134474.3.peg.4089; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_1_0_6; -.
DR Proteomes; UP000003395; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003670950"
FT DOMAIN 366..581
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 168
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 587 AA; 65571 MW; FFA6EA81F428375A CRC64;
MLNFFRWYFA LCVLFLSAAI TWANEPPRMT IDQTAATGVW ISDQGDGTYI NPVLQGDYSD
PDVVRVGDDF YLTSSSFTNV PGLPILHSKD LVNWKIISHA LQQIEPVAHH SVPRRGGGVW
APCIRHHNNQ FMIYYADPDF GVFVVTAKSA TGPWAKPQLI DSTKGVIDPC PFWEEGGKGY
MVYAYAHSRS GKSNIIELKE LAKDGLSVKG DGKIIIDGNL LPKVKTSYGD LPWFTLEGPK
LYKRKNYYYL FAPAGSVKGG WQAVFRAKHI TGPYEARSVM DQGDTTINGP HQGAWVNTAK
GEDWFLHFQQ TDSYGRRVLL QPMRWMADDW PIIGSPQKEN HFGQPVHSYK KPDAVVQIRQ
APIVNDEFNQ GFHLGWQWSA NPQSDWVDST ITNKLRLKSV SSPENLWEAG NLLTQKLPGM
RFTASTQFTL EPKRIGERAG LLVLGYNYGW IGLENTADGI RLVQVTRENA NLFAAETKLT
APLTVSGAVY VRIHIKPVIV AQPEPDYPVI YPSLLRAYHA QVTFSYSLDD THYYAIGPGF
IAQPGRWVGT QVGLFAQAAS GTPAYVATST GHAEFDYFRI ESGDKER
//
