ID B0SVS2_CAUSK Unreviewed; 521 AA.
AC B0SVS2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:ABZ71540.1};
DE Flags: Precursor;
GN OrderedLocusNames=Caul_2413 {ECO:0000313|EMBL:ABZ71540.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ71540.1};
RN [1] {ECO:0000313|EMBL:ABZ71540.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ71540.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP000927; ABZ71540.1; -; Genomic_DNA.
DR AlphaFoldDB; B0SVS2; -.
DR STRING; 366602.Caul_2413; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; cak:Caul_2413; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_1_0_5; -.
DR OrthoDB; 9801455at2; -.
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.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002755636"
FT DOMAIN 323..517
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 158
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 521 AA; 57042 MW; B348CDDD5087A507 CRC64;
MSKPFRRLTL AVAAGLGCLG AAATAQGQVW RADSGQGTYQ NPPLYADYPD PDIIRVGEDF
YFASTTFVNA PGLTILHSRD LVNWDIASHV MPRLEGNPKY DLREGGDYRH GLFAPSLRHH
NGRFYIAVTP VGHPTRIYSA ADIRGSWTVH ELDREAFDPG LFFDKDGRAF IVTSVGSDGT
IRLLTLNADL TAVTGEQKIH YVKGAEGSKL IRRGDWYYLF NSIPRRLALT VSRAKILTGL
WETREQIDDT TGGHQGALVD LPGGGWYGFV MRDAGAIGRV TNISPVFWRD DWPVWGTPDA
PGRVPDRAAK PILGKPFVEP PSSDDFKGRA LGRQWQWNHN PETSRWSLSA RPGFLRLQAT
KSADFWTARN TLIQKGQGPR SRAVVKLDVR ALAPGDACGF GTFGKFSNQL VVTRAPGGRG
AVSARVVEST ETGPATTPRG EARAIPLRNL WLSVDMDFSA DKAALAYSLD GRAWTAMPGD
FPLAFAWRTG TFQGEQFGLF CYNPAGGAGR LDVDSFTLSK P
//
