UL25_PSEXP
ID UL25_PSEXP Reviewed; 489 AA.
AC A0A1W2VMZ5; A0A1W2VMZ6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Ulvan Lyase-PL25 {ECO:0000303|PubMed:28290654};
DE EC=4.2.2.- {ECO:0000269|PubMed:28290654};
DE Flags: Precursor;
GN ORFNames=PLSV_3936;
OS Pseudoalteromonas sp. (strain PLSV).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1547444;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLSV;
RX PubMed=25502665; DOI=10.1128/genomea.01257-14;
RA Kopel M., Helbert W., Henrissat B., Doniger T., Banin E.;
RT "Draft genome sequence of Pseudoalteromonas sp. strain PLSV, an ulvan-
RT degrading bacterium.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0000312|PDB:5UAM}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF WILD-TYPE AND MUTANT HIS-123,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-123; TYR-188; ARG-204
RP AND HIS-264.
RX PubMed=28290654; DOI=10.1021/acschembio.7b00126;
RA Ulaganathan T., Boniecki M.T., Foran E., Buravenkov V., Mizrachi N.,
RA Banin E., Helbert W., Cygler M.;
RT "New ulvan-degrading polysaccharide lyase family: Structure and catalytic
RT mechanism suggests convergent evolution of active site architecture.";
RL ACS Chem. Biol. 12:1269-1280(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|PubMed:28290654}.
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 RefSeq; WP_033186995.1; NZ_JRKG01000030.1.
DR PDB; 5UAM; X-ray; 1.45 A; A/B=34-489.
DR PDB; 5UAS; X-ray; 1.60 A; A/B=34-489.
DR PDBsum; 5UAM; -.
DR PDBsum; 5UAS; -.
DR AlphaFoldDB; A0A1W2VMZ5; -.
DR SMR; A0A1W2VMZ5; -.
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 3D-structure; Cell membrane; Lipoprotein; Lyase; Membrane; Metal-binding;
KW Palmitate; Signal; Zinc.
FT SIGNAL 1..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 32..489
FT /note="Ulvan Lyase-PL25"
FT /id="PRO_0000448325"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:28290654"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:28290654"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28290654"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:28290654"
FT SITE 204
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000305|PubMed:28290654"
FT LIPID 32
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 32
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 123
FT /note="H->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28290654"
FT MUTAGEN 188
FT /note="Y->F: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28290654"
FT MUTAGEN 204
FT /note="R->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28290654"
FT MUTAGEN 264
FT /note="H->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28290654"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5UAM"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 237..251
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 256..267
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:5UAM"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 368..378
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 408..418
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 424..432
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 452..468
FT /evidence="ECO:0007829|PDB:5UAM"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:5UAM"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:5UAM"
SQ SEQUENCE 489 AA; 54275 MW; 24629F0A325D74E5 CRC64;
MNLNKTLRKN SPSGYKALLT FSIICGLMAT GCAHQESLPN STANSVDRQV GYFADNGVGN
PLAIVQHPAG IHKNGITYVS YQGPKEDPYI ASYNHQTGQW QGPFRAGISE LGRRDGGKKF
DNHGKPTMLI DDEGYIHIFY GGHGGQASNG KNPLGNTHHG ANKHAVSKRP YDISQWEDLN
NITPFGTYNQ AIKMDNGDIY LFFRHGAHRS DWVYQKSVDN GRTFASPVSF LKHKRRTDID
AVDSWYAWAG KGQGDNIIVS YDYHVCWDGG AGVNGRGHTT ERHDVYFMSF NTKTGEWSNV
EGEKLVLPVT REVADEKTMA MRTGELWTFN GSTHLDAQGQ PHIAINAGID KGAKTGGPKQ
TRHVRWNGNE WVGGDKVIPQ YERVSRGDFM VTDPENIRYL TTYNQDNDAV LSWWQSHDGG
EHFVEDKTVL RKDNASFAIS AFIKDAIPDA QMLVAEKVSD EGIKMYLVGE EGAVTRSLVD
LKTAMPTSK
