ID V4QQK3_9CAUL Unreviewed; 538 AA.
AC V4QQK3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xylosidase {ECO:0000313|EMBL:ESQ81468.1};
GN ORFNames=AEAC466_21290 {ECO:0000313|EMBL:ESQ81468.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ81468.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ81468.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ81468.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(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:ESQ81468.1}.
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DR EMBL; AWGE01000030; ESQ81468.1; -; Genomic_DNA.
DR RefSeq; WP_023460230.1; NZ_AWGE01000030.1.
DR AlphaFoldDB; V4QQK3; -.
DR STRING; 1282362.AEAC466_21290; -.
DR PATRIC; fig|1282362.3.peg.4193; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000017826; 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; cd09002; GH43_XYL-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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF2; XYLOSIDASE_ARABINOSIDASE; 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; PS51318; TAT; 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:UP000017826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004726018"
FT DOMAIN 360..536
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 172
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 538 AA; 59944 MW; 7D2EFA5E87C88FC4 CRC64;
MSQSNRRDAI KSMGLSAFLL GGVATARAAA EVPKEADIVT WAKGVEGKRR ADLGNGTFLN
PIMAGDHPDP SILKDGDDYY MTFSTFDAYP GLIIWHSTDL VNWQPIGPAL TQNIGSVWAP
ELCKHKGRFF LYIPTKKTSA AGSKTTSWVI WADDIKGPWS TPVDLDLPNH IDPGHAVGED
GTRWLFLSGG DRVRLSEDGL RRVGMPEHVY DPWHYPEDWD VEGFAPEGPK VTRHGDYFYL
ILAVGGTAGP PTGHMVIAAR SRSINGPWEQ HPRNPLVRTA SIKEKWWSRG HATLVEGPAG
DWWGVYHGYE NGYWTLGRQT LLAPVSWSND GWFDFGGGDL SLPIRKPRAG PPQPHGLALS
DDFETDKYGT QWNFFNPRPT ESGRIRRRDG VMHLTAAGEA PSNGAPLVFV TGDQAYEIEC
EIDIDPGTWA GLLLFYDQQL YCGLGFDEKA FVTHQYGIER GRPANPYGRR MLLRLRNDHH
IVSFHTSADG KIWKRFDRGM EVSGYHHNVR GGFLMLKPGL YAAGQGEARF KAFKYRAL
//
