ID A6LDZ6_PARD8 Unreviewed; 513 AA.
AC A6LDZ6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Glycoside hydrolase family 43, candidate beta-glycosidase {ECO:0000313|EMBL:ABR43910.1};
GN OrderedLocusNames=BDI_2179 {ECO:0000313|EMBL:ABR43910.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43910.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR43910.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP000140; ABR43910.1; -; Genomic_DNA.
DR RefSeq; WP_011966744.1; NC_009615.1.
DR AlphaFoldDB; A6LDZ6; -.
DR STRING; 435591.BDI_2179; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PaxDb; 435591-BDI_2179; -.
DR KEGG; pdi:BDI_2179; -.
DR PATRIC; fig|435591.13.peg.2162; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_543697_0_0_10; -.
DR BioCyc; PDIS435591:G1G5A-2237-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08999; GH43_ABN-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:SF5; ENDO-ARABINASE; 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:UP000000566};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002698774"
FT DOMAIN 330..472
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 143
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 513 AA; 57829 MW; 55E3DA25661386FE CRC64;
MRKIFTLFFC AASLATGLAQ QESYFTNPVI HGDVADPSII RIDQTYYITG TSSEWAPYYP
VFTSTDLVNW QQTGHVFDEK PEWTKSSFWA PEWYQHKGKV YVYYTARKQS DNISCIGVAV
ADSPTGKFKD HGPVVEFGKE AIDAFILEDK GKLYISWKAY GLDNQPIELL ACKLTDDGLR
LDGKPFSLLR DDERQGMEGQ HWFKKDGYYY IIYSVRGCCG PQSDYAVSVA RSKKLEGPYE
KYLGNPILHG SKEVLSIGHG TITTTPDGRM YYLCHAYQPG SGFYQGRQPY LQEVRMGEDH
WPHFVTGEYA SRTQPMPFAE SAQVPVFDFS DDFTGATLRP EWSWNYPYTD VKTEIKNGKL
SLSGTPKPGV KTGAALCLRP TSPNYTLETA IVNRNDSWKG ITMYGDANNL ITCGCAGDRL
ILKYILEGKE HQLADLPLPA SPLYLQMKVT DGTHSTFYWS KDGQAWNEIV GEALSAKETR
SLIQWDRISR PGLYQEGDPT APAVYAYCLL KNE
//