PLH24_FORAG
ID PLH24_FORAG Reviewed; 723 AA.
AC T2KMH0;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Beta-xylosidase {ECO:0000303|PubMed:31285597};
DE EC=3.2.1.- {ECO:0000269|PubMed:31285597, ECO:0000269|Ref.2};
DE AltName: Full=Glycosyl hydrolase 3 family protein P24 {ECO:0000305};
DE Short=P24_GH3 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P24 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P24;
DE Flags: Precursor;
GN ORFNames=BN863_22130;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1016/j.algal.2017.09.025;
RA Salinas A., French C.E.;
RT "The enzymatic ulvan depolymerisation system from the alga-associated
RT marine flavobacterium Formosa agariphila.";
RL Algal Res. 27:335-344(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: Xylosidase involved in ulvan degradation (Ref.2,
CC PubMed:31285597). Ulvan is the main polysaccharide component of the
CC Ulvales (green seaweed) cell wall. It is composed of disaccharide
CC building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-
CC glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl)
CC (Probable). Beta-xylosidase converts Xyl-Rha3S, a product of alpha-L-
CC rhamnosidase acting on Rha-Xyl-Rha3S oligosaccharides, further to Xyl
CC and Rha3S (PubMed:31285597). The enzyme is able to degrade 4-
CC methylumbelliferyl-beta-D-xylopyranoside (MUX) in vitro (Ref.2).
CC {ECO:0000269|PubMed:31285597, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79925.1; -; Genomic_DNA.
DR RefSeq; WP_038530516.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KMH0; -.
DR SMR; T2KMH0; -.
DR STRING; 1347342.BN863_22130; -.
DR EnsemblBacteria; CDF79925; CDF79925; BN863_22130.
DR PATRIC; fig|1347342.6.peg.2220; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_10; -.
DR OMA; GPTINTQ; -.
DR OrthoDB; 419160at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..723
FT /note="Beta-xylosidase"
FT /id="PRO_5004602849"
SQ SEQUENCE 723 AA; 79312 MW; A067675C23773AA3 CRC64;
MKKLWLMGLL LASFFTTVAQ NNAQTKSNSD EEIDKKVATL ISQMTLDEKI AEMTQDAPAN
ERLGIPSMKY GEALHGLWLV LDYYGNTTVY PQAVAAASTW EPELIKKMAS QTAREARALG
VTHCYSPNLD VYAGDARYGR VEESYGEDPY LVSRMGVAFI EGLQGTGEEQ FDENHVIATA
KHFVGYPENR RGINGGFSDM SERRLREVYL PPFEAAVKEA GVGSVMPGHQ DFNGVPCHMN
TWLLKDILRD ELGFDGFIVS DNNDVGRLET MHFIAENRTE AAILGLKAGV DMDLVIGKNV
ELATYHTNIL KDTILKNPAL MKYIDQATSR ILTAKYKLGL FDAKPKKIDT ETVETGTDEH
REFALELAEK SIIMLKNDNN LLPLDVSKIK SLAVIGPNAH EERPKKGTYK LLGGYSGLPP
YYVSVLDGLK KKVGEHVKIN YAKGCDIDSF SKEGFPEAIS AAKNSDAVVL VVGSSHKTCG
EGGDRADLDL YGVQKELVEA IHKTGKPVIV VLINGRPLSI NYIAENIPSI LETWYGGMRA
GDAVANVIFG DVNPGGKLTM SFPRDVGQVP VTYLERPDFI GSGKGQYRFS DKTPLFPFGF
GLSYTTFKYG TPKLDNTSIA ANGTTTVSVE VTNTGKVTGD EVVQMYVRDD YASVGRYLKM
LKGFKRITLK PGETKTVSFK LGFDELNILN QDLKKVVEPG TFTISVGASS KADDLKTVSL
TVK
