UL25_NONUL
ID UL25_NONUL Reviewed; 472 AA.
AC A0A084JZA8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Ulvan lyase;
DE EC=4.2.2.- {ECO:0000269|Ref.2};
DE Flags: Precursor;
GN ORFNames=IL45_03835, NLR_492;
OS Nonlabens ulvanivorans (Persicivirga ulvanivorans).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=906888;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22727 / CIP 110082 / PLR;
RX PubMed=25125644; DOI=10.1128/genomea.00793-14;
RA Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT "Draft genome sequence of Nonlabens ulvanivorans, an ulvan-degrading
RT bacterium.";
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: 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 the endolytic cleavage
CC of the glycosidic bond between Rha3S and the uronic acids GlcA or IduA,
CC producing oligosaccharides that have unsaturated 4-deoxy-L-threo-hex-4-
CC enopyranosiduronic acid (deltaUA) at the non-reducing end. This results
CC eventually in the degradation of the ulvan polysaccharide into deltaUA-
CC Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 25 family.
CC {ECO:0000305}.
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DR EMBL; JPJI01000023; KEZ94292.1; -; Genomic_DNA.
DR RefSeq; WP_036580476.1; NZ_PVNA01000004.1.
DR AlphaFoldDB; A0A084JZA8; -.
DR SMR; A0A084JZA8; -.
DR EnsemblBacteria; KEZ94292; KEZ94292; IL45_03835.
DR OrthoDB; 558664at2; -.
DR Proteomes; UP000028531; 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 InterPro; IPR036278; Sialidase_sf.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW Lyase; Metal-binding; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..472
FT /note="Ulvan lyase"
FT /id="PRO_0000448326"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT SITE 191
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
SQ SEQUENCE 472 AA; 53600 MW; 589D1BB9719925C5 CRC64;
MIIKQYLLKI SLCVLLLGCD SAKKEISKNE NSKTEVDYFA DNGFGNAVAL VQHPSGVYHN
GITYVAYQGP LEDPYVASYN HETKEWKGPF KAGISEMGKD PSRKKKIDNH GKPALLIDNA
GYVHIAFGGH GGMRHHGENT LGNYSYGKNL HAVSKKPYDI SEWETRDNVS LFGTYSQFIK
MDNGDIYLFY RHGAHRSDWV YQKSMDNGVT FSEPVSFLKH KRRTNIEAED SWYPWVSRGN
ADDIIVAFDY HICRDNVNAQ DARGHIPERH NVYYMVFDTK NGQWKNVKNE RLQMPLTKEM
ADEKTLVRSI PNDWTFQGIT DVDPDGNPHV AVLVGPDINA RRSGPKRLQH FRWDGQQWLK
SNTANLPRGD GDLEVTSATE VSIYLENKTS NDVGEISRWD SFNGGESFQK SKVFLQRENS
GFVISSLIDN PHPDARIIVA EKEEGTDFRK MYLLGDNGPI KRSKKEAQVL ND
