ID   PLH1_FORAG              Reviewed;         400 AA.
AC   T2KLZ3;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Unsaturated glucuronyl hydrolase {ECO:0000303|PubMed:31285597};
DE            Short=UGL;
DE            EC=3.2.1.- {ECO:0000269|PubMed:31285597};
DE   AltName: Full=Glycosyl hydrolase 88 family protein P1 {ECO:0000305};
DE            Short=P1_GH88 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P1 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P1;
DE   Flags: Precursor;
GN   ORFNames=BN863_21900;
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, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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: Unsaturated glucuronyl hydrolase involved in ulvan
CC       degradation (PubMed:31285597). Ulvan is the main polysaccharide
CC       component of the Ulvales (green seaweed) cell wall. It is composed of
CC       disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S)
CC       linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose
CC       (Xyl) (Probable). Unsaturated glucuronyl hydrolase catalyzes the
CC       cleavage of the unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic
CC       acid (deltaUA) at the non-reducing end of ulvan oligomers, thus forming
CC       5-dehydro-4-deoxy-D-glucuronate (PubMed:31285597).
CC       {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 88 family. {ECO:0000305}.
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DR   EMBL; HG315671; CDF79902.1; -; Genomic_DNA.
DR   RefSeq; WP_038530475.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KLZ3; -.
DR   SMR; T2KLZ3; -.
DR   STRING; 1347342.BN863_21900; -.
DR   EnsemblBacteria; CDF79902; CDF79902; BN863_21900.
DR   PATRIC; fig|1347342.6.peg.2197; -.
DR   eggNOG; COG4225; Bacteria.
DR   HOGENOM; CLU_027158_0_0_10; -.
DR   OMA; YWDLIFG; -.
DR   OrthoDB; 859760at2; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR010905; Glyco_hydro_88.
DR   Pfam; PF07470; Glyco_hydro_88; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..400
FT                   /note="Unsaturated glucuronyl hydrolase"
FT                   /id="PRO_0000448303"
FT   ACT_SITE        120
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RC92"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9RC92"
SQ   SEQUENCE   400 AA;  46416 MW;  D9755B9BEC764F23 CRC64;
     MRKLVYLVLV LGLTFLNVRC KSETKQNKKE EQNIGKQYSS LENRFQKLVN YPVGANNFPR
     SMSLAPEVVH KVPSKDWTSG FFPGNLWLIH ELTGDSIYKV KAQEWTVLME DQKENDRTHD
     MGFKVYCSFG EGLKQDPDNQ YYKDVIIESA KTLITRYNDT VKSIRSWDFN KDVWDFPVII
     DNMMNLELLF EATKISGDNI YHNIAVQHAN TTLKHQFRPD YSVFHVINYD TISGVVKTKD
     THQGFDRNST WARGQAWAIY GYTMSYRYTN NPKYLAQAEA TTQFYMEHEN LPKDGVPYWD
     FNDPEISDAP RDASAAAIVT SALFELYTYT NNKTYLDFAT QVLNTLNSEA YLLKDTVNGP
     FILNHSTGNW PKNDEIDEPI VYGDYYFLEA LKRKQNLILK