ID   UH105_ALTSL             Reviewed;         413 AA.
AC   P9WF04;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Unsaturated 3S-rhamnoglycuronyl hydrolase {ECO:0000305};
DE            EC=3.2.1.- {ECO:0000269|Ref.2};
DE   AltName: Full=Ulvan hydrolase;
DE   AltName: Full=Unsaturated beta-glucuronyl hydrolase;
DE            Short=UGL;
DE   Flags: Precursor;
GN   ORFNames=LOR_28;
OS   Alteromonas sp. (strain LOR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1537994;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LOR;
RX   PubMed=25342689; DOI=10.1128/genomea.01081-14;
RA   Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT   "Draft genome sequences of two ulvan-degrading isolates, strains LTR and
RT   LOR, that belong to the Alteromonas genus.";
RL   Genome Announc. 2:0-0(2014).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   DOI=10.1016/j.algal.2017.04.036;
RA   Foran E., Buravenkov V., Kopel M., Mizrahi N., Shoshani S., Helbert W.,
RA   Banin E.;
RT   "Functional characterization of a novel 'ulvan utilization loci' found in
RT   Alteromonas sp. LOR genome.";
RL   Algal Res. 25:39-46(2017).
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       the deltaUA-oligosaccharides deltaUA-Rha3S, deltaUA-Rha3S-IduA-Rha3S
CC       and deltaUA-Rha3S-Xyl-Rha3S, the end products of the ulvan lyase
CC       reaction. {ECO:0000269|Ref.2}.
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   RefSeq; WP_032096149.1; NZ_JQFW01000010.1.
DR   AlphaFoldDB; P9WF04; -.
DR   SMR; P9WF04; -.
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   Cell membrane; Hydrolase; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..413
FT                   /note="Unsaturated 3S-rhamnoglycuronyl hydrolase"
FT                   /id="PRO_0000448305"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O34559"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   413 AA;  46447 MW;  5C95A137F42C22C5 CRC64;
     MNHTKLKLSA VALTLALGLS ACSGESPEKQ VQSAESEQMK AVDVDKSMPM QSIESTAKRI
     GESAANWQIA QFGNLDYIPE SHRAKSENAK FWIQASFYIG LTRWIDATDD KQLESFVKQV
     AEKENYELIL ERPYHADDHA IAQTYLWLAE RAGVQEAYMP TKEVFDMILS KPPQVGLNMG
     DSESSSGKYH LEGNCQLRWC WADALFMAPR AWAQMTKVTS DPKYLEYGNK EFWAAADYLF
     SDEYGLFFRD SRYFDAKSDN GEPVFWGRGN GWVFAAIPMI IEELPEGHPS KDRYIELYKK
     HAEGLMALQK EDGYWPASLM DPDKVRTPEV SGTGFITFGL AWGVNNGILT DQRSKDVVEK
     GWSAITKAVT DDGRVNWVQH VGKSPDPVKE SDSQLYGTGA VLLAASEMLI WNK