UL24L_GLASK
ID UL24L_GLASK Reviewed; 1009 AA.
AC A0A2Z6UD27; A0A1Z4F651;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Ulvan lyase, long isoform;
DE EC=4.2.2.- {ECO:0000269|PubMed:28684315};
DE AltName: Full=Ulvan lyase A {ECO:0000303|PubMed:28684315};
DE Flags: Precursor;
GN Name=ullA; ORFNames=KUL10_22730 {ECO:0000312|EMBL:GBL04955.1};
OS Glaciecola sp. (strain KUL10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola; unclassified Glaciecola.
OX NCBI_TaxID=2161813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=KUL10;
RX PubMed=28684315; DOI=10.1016/j.bbrc.2017.07.003;
RA He C., Ohnishi K.;
RT "Efficient renaturation of inclusion body proteins denatured by SDS.";
RL Biochem. Biophys. Res. Commun. 490:1250-1253(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUL10;
RA Ohnishi K., Mondal R., Kobayashi S., Takahashi R.;
RT "Draft genome sequence of a ulvan-utilizing bacterium, Glaciecola sp.
RT KUL10.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ulvan lyase involved in ulvan degradation (PubMed:28684315).
CC Ulvan is the main polysaccharide component of the Ulvales (green
CC seaweed) cell wall. It is composed of disaccharide building blocks
CC comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid
CC (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl). Ulvan lyase
CC catalyzes preferentially the endolytic cleavage of the glycosidic bond
CC between Rha3S and the uronic acid GlcA, but not IduA, producing
CC oligosaccharides that have unsaturated 4-deoxy-L-threo-hex-4-
CC enopyranosiduronic acid (deltaUA) at the non-reducing end. The most
CC abundant end products in the degradation of the ulvan polysaccharide
CC were deltaUA-Rha3S disaccharides and deltaUA-Rha3S-IduA-Rha3S and
CC deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides (By similarity).
CC {ECO:0000250|UniProtKB:P9WF07, ECO:0000269|PubMed:28684315}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 mg/ml for ulvan {ECO:0000269|PubMed:28684315};
CC Vmax=60.6 umol/min/mg enzyme {ECO:0000269|PubMed:28684315};
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 24 family.
CC {ECO:0000305}.
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DR EMBL; LC278381; BAY00693.1; -; Genomic_DNA.
DR EMBL; BGNG01000006; GBL04955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6UD27; -.
DR SMR; A0A2Z6UD27; -.
DR EnsemblBacteria; GBL04955; GBL04955; KUL10_22730.
DR Proteomes; UP000247426; Unassembled WGS sequence.
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; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1009
FT /note="Ulvan lyase, long isoform"
FT /id="PRO_5016411667"
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 200
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 210
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 212
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 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 311
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 314
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 316
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 372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT SITE 247
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
SQ SEQUENCE 1009 AA; 112723 MW; 53255D4EE73DB8C5 CRC64;
MTAQKSKYFN RIMTMNTLLF SLLTVGFSQA YADVVLEKQV KITDDGLHFD GKDLNHGNID
SADPGEKYDF FFGPNISAHG DAVKTYKHYV FMTWYKGGKS ERNVMLSRYN TQTQTIATIE
FPHRHTGFRG NPLIGESHNT IGLAVSPNNG TIHMVYDLHA YDDNNHDGKF KDDFFRYSFS
VENAADLPDD QFTLDKFVKD TSSISQGPDD YKHISMTGDI ADKSNFARLT YPKFFTTTDG
TLLLYMRLGG NNNGAYVFNR YDEETQTWSK FTKFNENNQK NFGNPYNWGL YGNMKYVNGK
LRVGFQQRSS DNNDRYQYQN GVYYAYSDHP EGFGDWKNHK DDEITYPLVN SDEIKVLEPG
DYISHQEANS VYIVGSFDWT VTKKGDVHFI SKVRSTNRSR PDYEEEYLHS YKPAGADEFI
TTTDFTGASQ IYTAGDNIYI VGLKNGRPYV ERAKGGTNDF VRVYEATSGP VFDHGTLYIK
DGKVYYYLME KTSGNAMPLY LQIIDLDLES EANAPQVAFP STSLTVEQGY EQLSLGIDAT
SSIEGRTIES VTLYLNDELV RTDTTVPYLF GHASKPHETG AMGWKDEHEP NPNPLGPGEH
IFKAVAVDSE GDTGLATMRL TVQSNAPMVS FPTQLIEVDE GYEKLSVSVD ASSSVEGRTI
ESVTLFINGE EVRTDTTIPY LWGHGSKPHE TGAMGWREDH APNPNPFLAG EYVFTAIATD
SQGEQSETSM TLIVNGEATP PIVTWPNEVV TVTEGYKRLG ITIEAEASSE NATIESVTLY
RNDELVRVDT KYKWNFGHSF APYEFGAMGW LETHEPNPSP LLAGTHTFKV VAKDSTGLEG
EAFMTLIVLP PAGPSISFDE PDIELMTGYE SLSVSTYVAT VNESVDIISV ALFIDDVLVR
ENLEAPYVWG DANHPNELLS LEVGSYEFKA IARDTNDQVS EVSLLVSITL FGDFDGDNDV
DRTDVRAFSS AIRSGEALDQ RYDFNEDGVV DRSDTRGLTK ICSRPRCAS
