UH105_NONUL
ID UH105_NONUL Reviewed; 377 AA.
AC L7P9J4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Unsaturated 3S-rhamnoglycuronyl hydrolase {ECO:0000305};
DE EC=3.2.1.- {ECO:0000269|PubMed:24407291};
DE AltName: Full=Ulvan hydrolase {ECO:0000303|PubMed:24407291};
DE AltName: Full=Unsaturated beta-glucuronyl hydrolase {ECO:0000303|PubMed:24407291};
DE Short=UGL;
DE Flags: Precursor;
GN ORFNames=IL45_01505;
OS Nonlabens ulvanivorans (Persicivirga ulvanivorans).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=906888;
RN [1] {ECO:0007744|PDB:4CE7}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS)
RP OF 16-377, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=DSM 22727 / CIP 110082 / PLR;
RX PubMed=24407291; DOI=10.1074/jbc.m113.537480;
RA Collen P.N., Jeudy A., Sassi J.F., Groisillier A., Czjzek M.,
RA Coutinho P.M., Helbert W.;
RT "A novel unsaturated beta-glucuronyl hydrolase involved in ulvan
RT degradation unveils the versatility of stereochemistry requirements in
RT family GH105.";
RL J. Biol. Chem. 289:6199-6211(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22727 / CIP 110082 / PLR;
RX PubMed=25125644; DOI=10.1128/genomea.00793-14;
RA Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT "Draft genome sequence of Nonlabens ulvanivorans, an ulvan-degrading
RT bacterium.";
RL Genome Announc. 2:0-0(2014).
CC -!- FUNCTION: Glucuronyl hydrolase involved in ulvan degradation. Ulvan is
CC the main polysaccharide component of the Ulvales (green seaweed) cell
CC wall. It is composed of disaccharide building blocks comprising 3-
CC sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-
CC iduronic acid (IduA), or D-xylose (Xyl). Unsaturated 3S-
CC rhamnoglycuronyl hydrolase works together with ulvan lyases to fully
CC degrade the ulvan polymer, catalyzing specifically the cleavage of the
CC unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) of
CC deltaUA-Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S
CC tetrasaccharides, the end products of the ulvan lyase reaction. Also
CC hydrolases deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-GlcA-Rha3S
CC tetrasaccharidestetrasaccharides. Prefers tetrasaccharides over
CC disaccharides and prefers an uronic residue at subsite +2.
CC {ECO:0000269|PubMed:24407291}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:24407291};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:24407291};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24407291}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 105 family.
CC {ECO:0000305}.
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DR EMBL; JQ403607; AFQ98272.1; -; Genomic_DNA.
DR EMBL; JPJI01000012; KEZ94331.1; -; Genomic_DNA.
DR RefSeq; WP_036579431.1; NZ_PVNA01000009.1.
DR PDB; 4CE7; X-ray; 1.90 A; A/B/C=16-377.
DR PDBsum; 4CE7; -.
DR AlphaFoldDB; L7P9J4; -.
DR SMR; L7P9J4; -.
DR EnsemblBacteria; KEZ94331; KEZ94331; IL45_01505.
DR OrthoDB; 982403at2; -.
DR BioCyc; MetaCyc:MON-19227; -.
DR Proteomes; UP000028531; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 17..377
FT /note="Unsaturated 3S-rhamnoglycuronyl hydrolase"
FT /id="PRO_0000448304"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O34559"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4CE7"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:4CE7"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:4CE7"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 257..273
FT /evidence="ECO:0007829|PDB:4CE7"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 296..311
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:4CE7"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:4CE7"
SQ SEQUENCE 377 AA; 43817 MW; 92CA5EBCF162A884 CRC64;
MNKSILLLVT LLSLYSCTDT EKTPLEEKDV FNEDYIKTSM IKALEWQEAH PIFAIHPTDW
TNGAYYTGVA RAHHTTKNMM YMAALKNQAV ANNWQPYTRL YHADDVAISY SYLYVAENEK
RRNFSDLEPT KKFLDTHLYE DNAWKAGTNR SKEDKTILWW WCDALFMAPP VINLYAKQSE
QPEYLDEMHK YYMETYNRLY DKEEKLFARD SRFVWDGDDE DKKEPNGEKV FWSRGNGWVI
GGLALLLEDM PEDYKHRDFY VNLYKEMASR ILEIQPEDGL WRTSLLSPES YDHGEVSGSA
FHTFALAWGI NKGLIDKKYT PAVKKAWKAM ANCQHDDGRV GWVQNIGAFP EPASKDSYQN
FGTGAFLLAG SEILKMR
