ID   UL24L_PSEXP             Reviewed;        1001 AA.
AC   P9WF06;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Ulvan lyase, long isoform;
DE            EC=4.2.2.- {ECO:0000269|PubMed:26763234};
DE   Flags: Precursor;
GN   ORFNames=PLSV_3925;
OS   Pseudoalteromonas sp. (strain PLSV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1547444;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLSV;
RX   PubMed=25502665; DOI=10.1128/genomea.01257-14;
RA   Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT   "Draft genome sequence of Pseudoalteromonas sp. strain PLSV, an ulvan-
RT   degrading bacterium.";
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}.
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DR   RefSeq; WP_033186955.1; NZ_JRKG01000030.1.
DR   AlphaFoldDB; P9WF06; -.
DR   SMR; P9WF06; -.
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..1001
FT                   /note="Ulvan lyase, long isoform"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000448323"
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   1001 AA;  111366 MW;  3E3AC5705A5DA607 CRC64;
     MNGLKMLLFS TTLLTAFTLH AQVTLKQQVK ITDEGLHFDG RNLDFSNVGT PDTGEKYDFF
     FGPNISAHGD AVKTYKHYVF MTWYKGGKSE RNVMLSRYNT LSGELSTIEF PHRHTGFRGD
     PLVGESHNTI GLSVSPINGT IHMVFDMHAY DNNNHDGKFK DDFFRYSYSI AGAAELPHSE
     FTLDKFVKDT SEVSQGENDY KHLTMTGDLS DKGNFARLTY PKFFTTVDGT LLLYMRLGGN
     NNGAYVFNRY DAETETWSTF TKFNENNQKL KGNPYNWGLY GNMKYVNGKL RVGFQQRSND
     NSDKYKYQNG VYYAYSDHPD GFGDWKNHKG EPMTWPLINS DEIKVFEPGD YVSHTDANSV
     YIVGSFDWTV TEKGDIHIIS KVRSTDRSRP DYEEVYIHSY KPAGAEDFII STDFTGASEI
     YTSGDNVYIV GLEGGRPYVE KAQGGTNNFV RVYEASDGPT FDHGTLYIKD GKVYYYLMER
     TSGNAMPLYL QIIDLDLDLE SDANAPIVSF PSPSLTVEQG FEKLSLNIAA ESPVEVRTIQ
     SVTLYINDEL VRTDTSLPYL FGHGSKPHET GAMGWLDTHE PNPSPLPAGR HIFKAVAVDS
     EGDSSVATMM LTVNSNAPII SFPQESLEVD EGFEKLSLNI SAESAVEGRT IESVSLYIDG
     EFVRTDTSLP YLFGHASKPH ETGAMGWLDT HSPNPSPLTS GTYEFTAVAI DSEGEESTAT
     MQLVVKGEPE PPVVTWPNST VTVYEGYEKL AITIDAESPV EGRDIQSVTL YRNGELVRVD
     TRPVWNFGHS HAPYEFGAMG WLDRHDPNPA PLSVGTHTFT AVARDSAGLE TESDMTLIVL
     SLPGPSVMIN ESDISLLTEY QNLSITADAS TANDDTSLVS LALYIDDQLV REIYEPPFEW
     GADGYSNELL ELSEGSHLAR VVATDSNNKQ SESSIFINID LLGDLNKDSV VDKGDTRLFT
     AKLRAGETMD IRYDFNGDGV VNNRDTRGLI RRCTYSRCTS N