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Database: UniProt
Entry: P9WF03
LinkDB: P9WF03
Original site: P9WF03 
ID   RHA78_ALTSL             Reviewed;         920 AA.
AC   P9WF03;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Alpha-L-rhamnosidase {ECO:0000305};
DE            EC=3.2.1.40 {ECO:0000269|Ref.2};
DE   Flags: Precursor;
GN   ORFNames=LOR_34;
OS   Alteromonas sp. (strain LOR).
OC   Bacteria; Pseudomonadota; 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: Alpha-L-rhamnosidase 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). The enzyme is able to degrade
CC       p-nitrophenyl-alpha-L-rhamnopyranoside (PNP-Rha) in vitro. Incubating
CC       the enzyme with the products obtained after degradation with ulvan
CC       lyase and beta-glucuronyl hydrolase (i.e. the trisaccharides beta-
CC       alpha-L-Rha3S-IduA-Rha3S and beta-alpha-L-Rha3S-GlcA-Rha3S) showed no
CC       degradation, suggesting that the enzyme is active on neutral rhamnose
CC       and that desulfation of the oligosaccharide must be achieved before
CC       cleavage of rhamnose. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40; Evidence={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 78 family. {ECO:0000305}.
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DR   RefSeq; WP_032096153.1; NZ_JQFW01000010.1.
DR   AlphaFoldDB; P9WF03; -.
DR   SMR; P9WF03; -.
DR   OrthoDB; 9761045at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR33307:SF5; CELLULOSE-BINDING SDE182 NUCLEOSIDE HYDROLASE-LIKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF05592; Bac_rhamnosid; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..920
FT                   /note="Alpha-L-rhamnosidase"
FT                   /id="PRO_0000448312"
FT   ACT_SITE        506
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   ACT_SITE        779
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   BINDING         500
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   BINDING         504..506
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   BINDING         513
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   BINDING         565
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   BINDING         800
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   920 AA;  103904 MW;  D21A48150C885C2F CRC64;
     MCVVRTFWFA VLTVIFAVSC SSHSVIENDK PTSLKVGEGF VNPLGYYEAS PRFSWKPSIS
     NSKSTQQSAY QIQVSSTPEG LLTNPDKWDS EKIKSSAMSW VQYKGKKITS REKVFWRVRF
     WDENNIASQW SDVAHIEMGL LENLDWKASW IGAKDTESSL SPSQSTLATP QYLRTQFSVE
     KEVLEARLYV TAKGVFKVYL NGKDITANDA LPPGWTPYEK RIETLTYDVT TLITKRDNAL
     GAIIAGGWYS GRIADLKETD HSKPPRFLAQ LEITYSDNTT RLVTTNDSWK ATQSGPIRFA
     SNYDGERYDE TYEMQGWSMP DYDDSEWGTV ITDASTPGTL LRPKRHLPVR NVDKLTPLSF
     KQVSKDTVIF DFGQNMVGVP SIKLPVKQGK QVTLRFAEAL HKGDFYTDNY RSAHSTDYFL
     PAKDGIAEYT PTFTFHGFRF VEISGFDETK APVKNWIVAN VQHSDIDLYN NFLSANPKLN
     KLFENINWGL KGNFFDIPLD CPQRDERLGW TGDANAFIAP SMYMADVYGF WSAYLNSLRE
     EQTEDGFVPL YVPFVKWINW TSSGWGDAAT ILPWELYMMT GDQKILEDSY PSMKSWINYH
     DSQAKNNISS MMTFGDWLQP YPEAEGKGAN RGDTDFSLIS TAFFARSVAL TRKTALELGF
     NEDAKRYEVK QKTLAKAFRA EFFDEDLNVI KGKETQTAYL LALAFDLLPQ SEVNIAQTKL
     ISLLQSADTH LRTGFLGTPL LADVLQEAGR TDLVYELLFK ETYPSWFYSI NNGATTTWER
     WNSYSLEEGF NPQGMNSLNH YAYGTISRWF YEGILGVKPQ LPGFKKAIIS PQLTSKLGFA
     EGSIPTPSGD IDVSWTMTSD GFDVSVTVPF NISAEFVPPA HYSVVAATNA KNEPIKKWKG
     LKAGQYQFQL IIDEKHGGAQ
//
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