UL24L_ALTSL
ID UL24L_ALTSL Reviewed; 999 AA.
AC P9WF07;
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=Ulvan lyase, long isoform;
DE EC=4.2.2.- {ECO:0000269|PubMed:26763234};
DE Flags: Precursor;
GN ORFNames=LOR_61;
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 PubMed=26763234; DOI=10.1074/jbc.m115.673947;
RA Kopel M., Helbert W., Belnik Y., Buravenkov V., Herman A., Banin E.;
RT "New family of ulvan lyases identified in three isolates from the
RT Alteromonadales order.";
RL J. Biol. Chem. 291:5871-5878(2016).
CC -!- FUNCTION: Ulvan lyase involved in ulvan degradation. Ulvan is the main
CC polysaccharide component of the Ulvales (green seaweed) cell wall. It
CC is composed of disaccharide building blocks comprising 3-sulfated
CC rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid
CC (IduA), or D-xylose (Xyl). Ulvan lyase catalyzes preferentially the
CC endolytic cleavage of the glycosidic bond between Rha3S and the uronic
CC acid GlcA, but not IduA, producing oligosaccharides that have
CC unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) at
CC the non-reducing end. The most abundant end products in the degradation
CC of the ulvan polysaccharide were deltaUA-Rha3S disaccharides and
CC deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides.
CC {ECO:0000269|PubMed:26763234}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 24 family.
CC {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_032096165.1; NZ_JQFW01000010.1.
DR AlphaFoldDB; P9WF07; -.
DR SMR; P9WF07; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF63446; SSF63446; 1.
PE 1: Evidence at protein level;
KW Calcium; Lyase; Metal-binding; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..999
FT /note="Ulvan lyase, long isoform"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448322"
FT ACT_SITE 127
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 126..127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT SITE 236
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
SQ SEQUENCE 999 AA; 110898 MW; A2E1FD80B8F5C85B CRC64;
MKCLKTLLVS TTLLTAFSLN AEVTLEQQVK ITEEGLHFDG RNLDFSNVGT PDTGEKYDYF
FGPNISAHGD AVKTYRHYVF MTWYKGGKNE RNVMLSRYNT LNGELSTIEF PHKHTGFRGD
PLVGESHNTI GLSVSPINGT IHMVFDMHAY DNNNHGGKFK DDFFRYSFSV AGAAELPHSE
FTLDKFVKDT SEVSQGDDDY KHLTMTGDLD DKGNFARLTY PKFFTTVDGT LLLYMRLGGN
NNGAYVFNRY DAETESWSTF TKFNENNQKL KGNQYNWGLY GNMKYVNGKL RVGFQQRSND
NSDKYKYQNG VYYAYSDHPD GFGDWKNHKG EPMTWPLINS DEIKVFEPGD YISHTEANSV
YIVGSFDWTV TEKGDIHIIS KVRSTDRGRA DYEEVYIHSY KPAGAEEFII STDFPGASEI
YTSGDNVYIV GLEGGRPYVE KAQGGTNNFI RVYEASDGPV FDHGTLYIKD GKVYYYLMER
TSGTAMPLYL QIIDLDLESD ANAPIVSFPS PSVTVNQGYE KLSLNISAES PVEGRSIQSV
SLYIDDELVR TDDSLPFLFG HGSKPHETGA LGWLDRHEPN PSPLSAGRHV FKAVAVDSEG
DSSTATMILN VNSNAPIVSF PQESLEVDEG FERLSLNISA ESAVEGRTIE SVSLYIDGGL
VRTDTSLPYL FGHASKPHET GAMGWLDTHS PNPSPLAAGS YEFTAVATDN EGEETTASML
LVVKGEPEPP IVTWPNSTVT VYEGYEKLAI TIDAETPVEG RDIQSVTLFR NGELVRVDTR
PVWNFGHSFA PYEFGAMGWL DRHEPNPSPL GVGTHTFTAV ARDSAGLESE TDMALIVLSL
PGPSVMINEG DISLLTEYQN LAITAEASAA DDDISLVSLA LYIDEQLIRE IYEPPFIWGS
DAYSTELLSL TEGTHLVRVV ATDSNNKQSE SSIFINIDLL GDLNKDSIVD KADTRLFTSK
LRAGEIMDIR YDFNGDGVVN NRDTRGLVRR CTYSRCSSN
