ID A0A148KLA1_9ALTE Unreviewed; 581 AA.
AC A0A148KLA1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN ORFNames=AX660_01420 {ECO:0000313|EMBL:KXI27077.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27077.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI27077.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI27077.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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:KXI27077.1}.
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DR EMBL; LSNE01000015; KXI27077.1; -; Genomic_DNA.
DR RefSeq; WP_068381357.1; NZ_LSNE01000015.1.
DR AlphaFoldDB; A0A148KLA1; -.
DR STRING; 1799789.AX660_01420; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000070299; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000070299};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..581
FT /note="Beta-xylosidase C-terminal Concanavalin A-like
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007550176"
FT DOMAIN 394..577
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 179
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 581 AA; 64973 MW; 0CC620CBE82E06F3 CRC64;
MTSLFFRTCL LAASFPLLLA CQPNSAELDK NPKTPASVSF NWFEYQGNDE IFAQPLAQGQ
YQNPIVAGFY PDPSITRKGE DYYMVHSSFS YAPGVPILHS RDLVNWQLVG HILTQPTQLK
LDGLGVSRGI FAPTLRYHDG LFYMITTAVD SGGNFLVTAT DPAGPWSEPL WLPEIGGIDP
DIFFDDDGKV YIAHNDAPDG EPLYEGHRVI RLWEFDLATN TVVTSEGSGR VIVNGGVNIA
DKPVWIEGPH IYKINSWYYL TCAEGGTSVN HSQVVFRTKN LSEPFVPYAN NPILSQRDLD
PTRLNPVTST GHADFIQTAE GDWWSVFLAT RPYGDNFYNT GRETYLLPIT WQDEWPVILP
KGQEVPYRQI KPEINVELTQ LSATDALTGN FIWRDEFNQQ NIDPRWNFLR GFERSWLQVA
NDKLDMQASE FDLSSLQQTS FMGHRQQHGR FSLSTSLNLP AQQGISGGLT ALQNSAFYYY
FAVQKQQDNY RLFVQQVNNG QLSLLAETVI KAQAGQELTL LVNGDKGHIS FSYKLADGEQ
VEVVSNADAT LLSTERAGGF VGAMLGLHVR NEPSSNNKQV D
//