RHA78_ALTSL
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 03-AUG-2022, entry version 7.
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; 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; WP_032096153.1; NZ_JQFW01000010.1.
DR AlphaFoldDB; P9WF03; -.
DR SMR; P9WF03; -.
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; 2.60.40.10; -; 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 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; 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..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
