PLH17_FORAG
ID PLH17_FORAG Reviewed; 981 AA.
AC T2KN75;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Beta-glucuronidase {ECO:0000305};
DE EC=3.2.1.31 {ECO:0000269|PubMed:31285597};
DE AltName: Full=Glycosyl hydrolase 2 family protein P17 {ECO:0000305};
DE Short=P17_GH2 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P17 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P17;
GN ORFNames=BN863_22060;
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 X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION,
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: Beta-glucuronidase involved in ulvan degradation
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-glucuronidase removes GlcA side chains present on some
CC O2 residues of Rha3S. Can remove the GlcA side chains from polymeric
CC ulvan or from smaller oligomers (PubMed:31285597).
CC {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
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:0000269|PubMed:31285597};
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 2 family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79918.1; -; Genomic_DNA.
DR PDB; 6HPD; X-ray; 2.43 A; A=19-981.
DR PDBsum; 6HPD; -.
DR AlphaFoldDB; T2KN75; -.
DR SMR; T2KN75; -.
DR STRING; 1347342.BN863_22060; -.
DR EnsemblBacteria; CDF79918; CDF79918; BN863_22060.
DR PATRIC; fig|1347342.6.peg.2213; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_3_0_10; -.
DR OMA; PMWAMEY; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
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; PF18565; Glyco_hydro2_C5; 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 SUPFAM; SSF49303; SSF49303; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Magnesium; Metal-binding; Periplasm;
KW Reference proteome.
FT CHAIN 1..981
FT /note="Beta-glucuronidase"
FT /id="PRO_0000448301"
FT ACT_SITE 500
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:31285597"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 562
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 563
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 581
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31285597"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 220..233
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 269..280
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 407..424
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 430..438
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 535..549
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 620..636
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 639..644
FT /evidence="ECO:0007829|PDB:6HPD"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 652..659
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 662..671
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 674..682
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 687..695
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 708..717
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 728..740
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 755..760
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 763..770
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 775..782
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 789..796
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 841..847
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 864..869
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 884..888
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 900..916
FT /evidence="ECO:0007829|PDB:6HPD"
FT HELIX 923..928
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 930..938
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 941..950
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 955..958
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 961..964
FT /evidence="ECO:0007829|PDB:6HPD"
FT STRAND 974..979
FT /evidence="ECO:0007829|PDB:6HPD"
SQ SEQUENCE 981 AA; 111684 MW; 9E788F28A18AEAA3 CRC64;
MTILCSCAQQ QQQQQQDTEV ITSSERTTYN FNVDWKFIKS NPKQAQDINY NDATWETISC
PHTFNDVDTF DDLSHGHHDG EDNQWRGTVW YRKHFKLPKD DKGKKVFIEF ESVRQIADVY
INGVHLGQNQ TGFIPFGFDL TPHLKFGEEN IIAVKVNNDR GDHFRENFPL VWNHEHWHPT
HGGIYRNVFL HTMDPLHITL PLYDNLETVG TYVYAENISE KSADITVETE IQNEHAENKN
ITLVTQIVDN DGAVVAHSNK NVAIPSGQKM KVTTVTNIQN PQLWYTRYPY MYKVVSAIKE
SNKVIDTYES PLGIRNFDFN KDSGFWINGE QIKLHGWGQK PTNAWAGLGA ALPDWLRDFT
FKLMDEAGGN FIRWGHCAAS PAEVDMGDKY GFVTLMPGVS GESEDEGETW DIRYKAFKDL
IVYYRNHPSI FIWEGGNWAE SEAHYKEILE AIKTFDPKGK RLMGNRRADV KNDSEGYVSI
EIGTEGWERE YPDLPIIESE YNREEAPRRI WDKNSPDDNF YNHPNISKNT YKLSSEEFAV
RQADHWWNKM GKKAYHSGGA NWIFSDGPHG GRCPTEVTRA SGEVDAVRLP KEAFYALKAM
WRPEPQVHIV GHWNYEVGTK KTMYVMSNCA SVKLYVNDKL VGTNSNPENG YVFKFDNVAW
ESGKIKAEGF IDDALKTTQT KETTGEPAAL KLTSITGPEG WLADGSDVAL IDVEVVDAQG
RRCPLAKGRV DFTISGPAIW RGGYNSGKPN STNNLFLDIE AGINRVAVRS VLESGTVTIM
AKKPGFKDVS VTLKSLPIDF NNGLTTTLPQ VYTNVLTKEP LPEHIPEMPE YIPGVKNRSE
LFRKFSYTGD GKAMLRTNMH WGKKAYTDLE YNYTVLPRYL NESEYVRTPN SDNRYWARDQ
LQFIAGKKMH IYVLHDDTVP RPEFLLRDYE DTGDNVNVVG ASMSVFHRVA EEGESIIMAG
NSDGDAPENC RMYTVMVKEF K
