ID A0A086A3X2_9FLAO Unreviewed; 569 AA.
AC A0A086A3X2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KFF11386.1};
GN ORFNames=IW15_16750 {ECO:0000313|EMBL:KFF11386.1};
OS Chryseobacterium soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF11386.1, ECO:0000313|Proteomes:UP000028705};
RN [1] {ECO:0000313|EMBL:KFF11386.1, ECO:0000313|Proteomes:UP000028705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF11386.1,
RC ECO:0000313|Proteomes:UP000028705};
RA Stropko S.J., Pipes S.E., Newman J.;
RT "Genome of Chryseobacterium soli DSM 19298.";
RL Submitted (JUL-2014) 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:KFF11386.1}.
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DR EMBL; JPRH01000007; KFF11386.1; -; Genomic_DNA.
DR RefSeq; WP_034713432.1; NZ_JPRH01000007.1.
DR AlphaFoldDB; A0A086A3X2; -.
DR STRING; 445961.IW15_16750; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000028705; 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.
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..569
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001802138"
FT DOMAIN 391..562
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 174
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 569 AA; 63503 MW; 10E1EF1C5FFBA355 CRC64;
MKKRLIHPIV FKNKAVLAVT ALLSLNISAQ VFSGFTYRGN DKIYTDNPLK DDEFYSPVLQ
GCYPDPSITR KGNDYYLVNS SFSMFPGVPI FQSKDLVNWK QIGHVLDRPS QLKVEKSGVS
EGIYAPDIKY NPYNDTFYMV TTQIASGIGN MIVKTKDPTK GWSEVQKLNF DGIDPSIFFD
DNGKAYIIHN DAPPKGTEQY SGHRVIKIWD YDLEKDQVVA GTDKIIVNGG VDLSQKPIWI
EGPHLYKKRG KYYLMCAEGG TGGNHSEVIF VSDSPKGPFI PAGNNPILTQ RYFPKDRKDK
VDWAGHADLV ETPEGDYYGV FLAIRPNEKN RVNTGRETFI LPVDWSGTYP VFQNGLVPIK
PALKMLKGVK NQTGQTGFFP NGNFTFSDAL TNSDLDKRWI AMRGPRENFI TITKKGLKIN
SFATNIKAKA PISALFHRQQ HASFEAAVAL DFTPKSEKEL AGITCYQNEK FNYVFGLTKK
GNDYYLVLER TEKGNSIIVA HEKIGLSKTM QLKVVAEGDD YTFNYSLDGK TFKNLGGKVS
GDILSTDIAG GFTGSLIGLY STLSNDMNW
//
