ID V7EF10_9RHOB Unreviewed; 530 AA.
AC V7EF10;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:ESW59543.1};
GN ORFNames=Q27BPR15_16950 {ECO:0000313|EMBL:ESW59543.1};
OS Rhodobacter sp. CACIA14H1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW59543.1, ECO:0000313|Proteomes:UP000018503};
RN [1] {ECO:0000313|EMBL:ESW59543.1, ECO:0000313|Proteomes:UP000018503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24435858;
RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T.,
RA Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a
RT Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a Cyanobium
RT Species.";
RL Genome Announc. 2:e01116-13(2014).
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:ESW59543.1}.
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DR EMBL; AYNO01000160; ESW59543.1; -; Genomic_DNA.
DR AlphaFoldDB; V7EF10; -.
DR STRING; 1408890.Q27BPR15_16950; -.
DR PATRIC; fig|449393.3.peg.3385; -.
DR Proteomes; UP000018503; 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; cd09000; GH43_SXA-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 Reference proteome {ECO:0000313|Proteomes:UP000018503}.
FT DOMAIN 326..523
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 303..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 126
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 530 AA; 59317 MW; AA289FA1CCE79D46 CRC64;
MLQNPILPGF NPDPSICRVG GDYYIATSTF EWYPGVQIHH STDLVNWELV ARPLRRPAQL
DMRGNPDSCG VWAPCLSHDG ERFWLVYTDV KRFDGAFKDA HNYIVTCDTI DGDWSDPTYV
TSSGFDPSLF HDDDGRKWFL NMRWNHRGKG TGLNPAHDSF DGIELQEWHH VHGLTGPVHT
IFTGSPLGLT EAPHLFKKNG WYYLTTAEGG TGYDHAVTMA RSRSITGPYE MHPDTHLLTT
RFTPDHPLQR VGHGQYVETP EGQGFHTFLC GRPLPGNFCP LGRETGLARI DWHDDGWPRL
ADGGMAPPPT IDLPAKRRPD RPIHRSFQTR DLPPEFQWLR TPYPERLFTL TGQALRLTGR
ESLGSFFEQA LVARRQEHHA YTAATVVMAD PPDWQRAAGL ITYYNRHKFH AALVTREAAY
GRCLTLVSCL GDWPGEALTF HYHHPLAEGP VRIEVQVDGP TQRFLVATGD APMHPVGPTL
DASLISDEGG RGEHANFTGA FVGMVAHDLT GQGWTADFLR FDYIPSKGGA
//
