UL25_ALTSL
ID UL25_ALTSL Reviewed; 485 AA.
AC P9WF05;
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;
DE EC=4.2.2.- {ECO:0000269|Ref.2};
DE Flags: Precursor;
GN ORFNames=LOR_29;
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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 25 family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P9WF05; -.
DR SMR; P9WF05; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Lyase; Membrane; Metal-binding; Palmitate;
KW Signal; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 34..485
FT /note="Ulvan lyase"
FT /id="PRO_0000448324"
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT SITE 208
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A1W2VMZ5"
FT LIPID 34
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 34
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 485 AA; 53712 MW; 15D2C973D98087CB CRC64;
MIRNDTMLKG QFVLKKTQIA LSAALMGSVL LTGCVTQKSN TESNGPKDTQ VSYVEYFADN
AVGNPLAIVQ HPAAIHKNGI TYVSYQGPKE DPFVATYNHS TKEWSGPFKA GTSELGRRDG
GKKFDNHGKP TMLIDDEGYV HIFYGGHGGH SSNGKNPLGN THFGANKHAV SKKPYDITQW
EDLDNITPFG TYNQVVKMDN GDIYLFFRHG AHRSDWVYQK SVDNGRTFSS PVSFLKHKRR
TDIEAVDSWY AWVGKGEGDN LIVSYDYHVC WDGGAGINGR GHTTERHDVY FMNFNTKTNQ
WSNVEGESLA LPVTKEVADD KTLAMKTGAL WTFNGTSHLD NEGHPHIAIN AGVDRGAKTG
GPKQTRHVWW DGKKWLGGNN IIEGYQGVSR GDFRVTDPSD IRYLVTYEKE GDAVLSWWDS
DEDGNAFSEG STVLRKNNAT FAISALIENA HPEAQMLVAE KESDENIKIY LVGEDGPVPR
ALSNL
