UL24S_ALTSL
ID UL24S_ALTSL Reviewed; 528 AA.
AC A0A109PTH9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Ulvan lyase, short isoform;
DE EC=4.2.2.- {ECO:0000269|PubMed:26763234};
DE Flags: Precursor;
GN ORFNames=LOR_107;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=LOR;
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).
RN [2]
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 [3]
RP FUNCTION.
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).
RN [4] {ECO:0007744|PDB:6BYP, ECO:0007744|PDB:6BYT, ECO:0007744|PDB:6BYX}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-528, AND MUTAGENESIS OF
RP HIS-152; HIS-173; TYR-249; ARG-265 AND ARG-326.
RX PubMed=29382716; DOI=10.1074/jbc.ra117.001642;
RA Ulaganathan T., Helbert W., Kopel M., Banin E., Cygler M.;
RT "Structure-function analyses of a PL24 family ulvan lyase reveal key
RT features and suggest its catalytic mechanism.";
RL J. Biol. Chem. 293:4026-4036(2018).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:26763234};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:26763234};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26763234}. Cell
CC membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 24 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KU168251; AMA19991.1; -; Genomic_DNA.
DR PDB; 6BYP; X-ray; 1.90 A; A/B=32-528.
DR PDB; 6BYT; X-ray; 2.20 A; A/B=32-528.
DR PDB; 6BYX; X-ray; 2.21 A; A/B=32-528.
DR PDB; 6JQ9; X-ray; 1.81 A; A/B=45-527.
DR PDBsum; 6BYP; -.
DR PDBsum; 6BYT; -.
DR PDBsum; 6BYX; -.
DR PDBsum; 6JQ9; -.
DR AlphaFoldDB; A0A109PTH9; -.
DR SMR; A0A109PTH9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Lipoprotein; Lyase; Membrane;
KW Metal-binding; Palmitate; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 30..528
FT /note="Ulvan lyase, short isoform"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000448321"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:29382716"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:29382716"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29382716"
FT SITE 265
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000305|PubMed:29382716"
FT LIPID 30
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 30
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 152
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29382716"
FT MUTAGEN 173
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29382716"
FT MUTAGEN 249
FT /note="Y->F: Greatly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:29382716"
FT MUTAGEN 265
FT /note="R->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29382716"
FT MUTAGEN 326
FT /note="R->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29382716"
FT STRAND 49..61
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6BYP"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 183..190
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:6JQ9"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 306..315
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 318..328
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6BYP"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6BYT"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6JQ9"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 501..508
FT /evidence="ECO:0007829|PDB:6JQ9"
FT STRAND 511..523
FT /evidence="ECO:0007829|PDB:6JQ9"
SQ SEQUENCE 528 AA; 59635 MW; 6A362C8EE9F7F537 CRC64;
MKINLSMREL VSRLSTTLKT AIALSVLTAC TANDSVSLTS NISNTSGVLL ESQTKITDGA
LHFDGKKLNH NTFENPSKSQ AYDYFFGRNI SAHGDAVKPY KHFVFMTWYK GGKEERNVML
SRFNTKTGVV KTIQFPHRHT GFRGDPLVGE SHNTIGLAVS PLNGTIHMVY DMHAYVDDDE
TGRFKGRFVD DFFRYSFSVA GAADVPDDEF TLEQFVKDTS ELSQGADDYK HLTMTGNLQD
KENFSALTYP KFYTSDDGEL LHYMRWGGNN NGAYYFNKYD AKNQKWTRFT PFNHKDQKTH
GNAYNWGLYG QMKYINGKLR VGFQQRSANN DDRFKYQNGV YYAYSDHPDG LGNWKNVDGE
DMTWPLVNSD EIKIFEPGDY IDHTAPNSVH IVTGFDWTVT ENDDVHFITH VRSTDTKRSD
YKEVSIHAFK PANAVDFTIT TDFTGADSIY TSGDSIFIIG LKNGYPFVEK AKGGSNDFEV
VYQQASGVKF DHGTIHIENG KAYYYLMEKG AGNALPLHLQ VIDLGVTE
