ID   PLH16_FORAG             Reviewed;        1034 AA.
AC   T2KM09;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 2.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Putative beta-glucuronidase {ECO:0000305};
DE            EC=3.2.1.31 {ECO:0000250|UniProtKB:P05804};
DE   AltName: Full=Glycosyl hydrolase 2 family protein P16 {ECO:0000305};
DE            Short=P16_GH2 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P16 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P16;
GN   ORFNames=BN863_22050 {ECO:0000312|EMBL:CDF79917.1};
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   REVISION OF GENE MODEL.
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, 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: Glycoside hydrolase that may be involved in ulvan degradation
CC       (Probable). Ulvan is the main polysaccharide component of the Ulvales
CC       (green seaweed) cell wall. It is composed of disaccharide building
CC       blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic
CC       acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
CC       {ECO:0000305|PubMed:31285597, ECO:0000305|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC         Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC         Evidence={ECO:0000250|UniProtKB:P05804};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:31285597}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CDF79917.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR   EMBL; HG315671; CDF79917.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; T2KM09; -.
DR   SMR; T2KM09; -.
DR   STRING; 1347342.BN863_22050; -.
DR   EnsemblBacteria; CDF79917; CDF79917; BN863_22050.
DR   PATRIC; fig|1347342.6.peg.2212; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_0_1_10; -.
DR   OrthoDB; 1832114at2; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR026876; Fn3_assoc_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF13287; Fn3_assoc; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..1034
FT                   /note="Putative beta-glucuronidase"
FT                   /id="PRO_0000448300"
FT   DOMAIN          909..1034
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P05804"
SQ   SEQUENCE   1034 AA;  117464 MW;  56F7CE10EBF7C731 CRC64;
     MHQKIVECIP LWSRNLNSNV KGMRGEGIAC LLIVLCSIIY RTEAQRIETN FNNNWHFILK
     DSPDFSKENL DDSSWELLNV PHDWSFEKGV RKGGDQGQGG GYHDGGIGWY RKTFSFSKAS
     LSKTTYINFD GVYMNSEVWI NGNRLGKRPY GYISFRYDIS KYLKVGKNTI AVRVDNGLEP
     SARWYHSCGI YAPVKLVEVN PTHFKPNTIF IKTPSIEKQQ GVVSIDAEIK GAFKGLKYNV
     ELLTANGKVI ATHSEKLASA QPSVQLEVKP PKLWSPESPN LYKAKTQILD GKKVIDEKTT
     TFGFRTVAWK TETGFWLNGE NVKLKGVCEH WEGGPVGGAW TKPMLRWKLQ SLKDMGINAI
     RPSHNSTPPM FYDICDEIGL LVMDEIFDGW HKKAPEDYGK QAFDEWWQAD VKEWITRDRN
     HPSIFVWSLG NETHSDVAPE MVAFGKNLDP TRLFTSGAGN PEDMDIQGVN GGSETKSFIE
     NNKLTKPFIS TEAPHTWQTR GYYRTQTWWR DNELSGTYEL PNLTEKEVFF YEGINPKNWK
     NRKQRFNSSY DNATVRVSAR KYWEVMRDTP WHSGHFRWTG FDYYGEAGLV HGGLPFNLFM
     GGALDVAGFK KDLYYFYQSQ WTEKPMIHML PHWTHPRMKK GTVIPVWVYA NADEVELFLN
     GISLGKDKPG TVWNEMQCEW LVPYEEGTLE AVGYINGKVV NRTSFSTAQQ PSKLKTSILK
     LDAEGSFTDS FIVTSESLDT AGHLYPYGEN KVYYHIQGDV KKISMENGNP IDPTSRTKSD
     FRALFFGKTR TFLRALPEPK EAAVVTAAIL GDKALYTSNL ITIDAQHIQL LGKSKTSDLE
     IRYTTNGENP ETHGKLYKDA FMVEDDTTVK AIVKQNGKTV LSMEETFGKN EGLFWGDEHS
     ADMWIGRGVD ISAEEGVLTG AAKPSREAHR FKGSGFVDFK GGEGSITWYQ ENDGEPGDYS
     IRFRYMHNNH GKLHPMKLYV NDEYVRTIEF EPTGGWEKEW KFVPTIIVLQ SGANNIKLET
     TGESGPFIDE LFID