ID A0A1V9G190_9BACT Unreviewed; 534 AA.
AC A0A1V9G190;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:OQP64352.1};
GN ORFNames=A3860_20485 {ECO:0000313|EMBL:OQP64352.1};
OS Niastella vici.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP64352.1, ECO:0000313|Proteomes:UP000192796};
RN [1] {ECO:0000313|EMBL:OQP64352.1, ECO:0000313|Proteomes:UP000192796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ57 {ECO:0000313|EMBL:OQP64352.1,
RC ECO:0000313|Proteomes:UP000192796};
RA Chen L., Wang D., Yang S., Wang G.;
RT "Niastella vici sp. nov., isolated from farmland soil.";
RL Submitted (MAR-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:OQP64352.1}.
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DR EMBL; LVYD01000042; OQP64352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9G190; -.
DR STRING; 1703345.A3860_20485; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000192796; 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 Reference proteome {ECO:0000313|Proteomes:UP000192796};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010717989"
FT DOMAIN 341..534
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 213
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 155
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 534 AA; 59474 MW; 0948A223605A0B49 CRC64;
MKKLFVLGFT CISLYATAQQ PYVSKVWVAD NKNGTYKNPV LYADYSDPDA CRVGDDYYLV
ASSFDGIPGL PILHSKDLVN WTIIGHALKR QPPFDHFSQP RHGMGVWAPA IRFHNGEFYI
YYPDPDFGIY VVKAKSINGP WTEPMLVEGG KGLIDPCPLW DDDGKVYLVH AYAGSRAGIK
SIVVVKRLDA TGTKVMDGGA MVFDGHDQDP TLEGPKIYKR NGYYYIFAPA GGVATGWQLV
LRSKSIYGPY ERKVVMDQGG STINGPHQGA WVDTKTGEDW FLHFQDLEAY GRVVHLQPMK
WVNNWPVIGV DKDGDGKGEP VLQYKKPNVG KNYPVQTPPE SDEFNGHTMG LQWQWQANPK
PYWAFPGNGY LRLFSGQVSD TAKNLWFVPN VLMQKLPAPE FTATVKLDFK PRLAGEKTGL
IIMGSDYAYI GLTKKEDGIY LSYVICKGAE AGKPEQEKII AKITSATSYL RVQISKGAKC
SFTYSEDGQH FSEAGEVFTA VPGRWIGAKI GLFCTRTVVT NDSGFADVDW FRIE
//
