UL24L_ALTSX
ID UL24L_ALTSX Reviewed; 999 AA.
AC A0A1Z4F647;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, 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:28958183};
DE AltName: Full=Ulvan lyase A {ECO:0000303|PubMed:28958183};
DE Flags: Precursor;
GN Name=ullA {ECO:0000303|PubMed:28958183};
OS Alteromonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-36, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY ULVAN.
RC STRAIN=KUL17;
RX PubMed=28958183; DOI=10.1080/09168451.2017.1379352;
RA He C., Muramatsu H., Kato S.I., Ohnishi K.;
RT "Characterization of an Alteromonas long-type ulvan lyase involved in the
RT degradation of ulvan extracted from Ulva ohnoi.";
RL Biosci. Biotechnol. Biochem. 81:2145-2151(2017).
CC -!- FUNCTION: Ulvan lyase involved in ulvan degradation (PubMed:28958183).
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:28958183}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.2 mg/ml for ulvan {ECO:0000269|PubMed:28958183};
CC Vmax=185 umol/min/mg enzyme {ECO:0000269|PubMed:28958183};
CC -!- INDUCTION: By ulvan (at protein level). {ECO:0000269|PubMed:28958183}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 24 family.
CC {ECO:0000305}.
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DR EMBL; LC278382; BAY00694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4F647; -.
DR SMR; A0A1Z4F647; -.
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; Direct protein sequencing; Lyase; Metal-binding; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:28958183"
FT CHAIN 22..999
FT /note="Ulvan lyase, long isoform"
FT /id="PRO_5012644910"
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; 110838 MW; 93EB8764B9924EFA CRC64;
MKCLKTLLVS TTLLGAFSLN AEVTLEQQIK ITDEGLHFDG RNLDFSNVGS PDTGEKYDYF
FGPNISAHGD AVKTYKHYVF MTWYKGGKNE RNVMLSRYNT LSGELSTIEF PHRHTGFRGD
PLVGESHNTI GLAVSPINGT IHMVFDMHAY DDNNHGGKFK DDFFRYSYSV PGAAELPHSE
FTLDKFVKDT SEVSQGDDDY KHLTMTGDLG DKGNFARLTY PKFFTTVDGT LLLYMRLGGN
NNGAYVFNRY DAEAEKWSTF TPFNENNQKS KGNPYNWGLY GNMKYINGKL RVGFQQRSSD
NTDKYKYQNG VFYAYSDHPD GFGDWKNHKG EPMTWPLINS DEIKVFEPGD YISHTEANSV
YIVGSFDWTV TEKGDIHIIS KVRSTDRNRP DYEEVYIHSY KPAGADEFII STDFTGASEI
YTSGDNVYIV GLEGGRPYVE KAQGGTNNFV RVYKATDGPV FDHGTLYIKD GKVYYYLMER
TSGNAMPLYL QIIDLDLESD ANAPLVSFPS PSLTVEQGFE KLSLNISAES PVEGRFIQSV
SLYINDELVR TDDSMPYLFG HGSKPHETGA MGWLDTHEPN PSPLPAGTHI FKAVAVDSEG
DSAIATMVLN VNSNAPIVSF PQESLEVDEG FEKLSLNISA ESAVEGRSIE SVSLYINGEL
VRTDTSLPYL FGHASKPHET GAMGWLDTHS TNPSPLTAGT YEFTAVAIDS EGEESTASMQ
LVVKGEPQPP AVTWPNSTVT VYEGYEKLAI TIDAESPVEG RDIQSVTLYR NGELVRVDTR
PVWNFGHSFA PYEFGAMGWL DRHEPNPSPL GVGTHTFTAV AKDSTGLEGE SDMTLIVLSL
PGPSITINES DVSLLTEYQN LAITADASTA NDDITIVSLA LYLNEQLVRE IYEPPFEWGG
ENYSDELLDL PVGTHLAKVV ATDSNNNQTE ASMFVTIELL GDLNKDSVVD NKDIRLFTAA
LRNGEEMNIR YDFNDDGVVN NRDTRGLVHR CTYSRCGSN
