UL24S_PSEXP
ID UL24S_PSEXP Reviewed; 528 AA.
AC A0A0X9SHN5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Ulvan lyase, short isoform;
DE EC=4.2.2.- {ECO:0000269|PubMed:26763234};
DE AltName: Full=PsPL;
DE Flags: Precursor;
GN ORFNames=PLSV_3875;
OS Pseudoalteromonas sp. (strain PLSV).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1547444;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=PLSV;
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=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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1039/C7RA12294B;
RA Qin H.-M., Xu P., Guo Q., Cheng X., Gao D., Sun D., Zhu Z., Lu F.;
RT "Biochemical characterization of a novel ulvan lyase from Pseudoalteromonas
RT sp. strain PLSV.";
RL RSC Adv. 8:2610-2615(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 Kinetic parameters:
CC KM=2.1 mg/ml for ulvan {ECO:0000269|Ref.3};
CC Note=kcat is 7.08 sec(-1) with ulvan as substrate.
CC {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:26763234, ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius (PubMed:26763234). Optimum
CC temperature is 35 degrees Celsius (Ref.3).
CC {ECO:0000269|PubMed:26763234, ECO:0000269|Ref.3};
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 24 family.
CC {ECO:0000305}.
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DR EMBL; KU168252; AMA19992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X9SHN5; -.
DR SMR; A0A0X9SHN5; -.
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 Calcium; Cell membrane; Lipoprotein; Lyase; Membrane; Metal-binding;
KW Palmitate; 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_5007072402"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 218
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 228
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 230
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 309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT BINDING 329
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 332
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 334
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 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
FT SITE 265
FT /note="Neutralizes the sugar carboxylate group at subsite
FT +1"
FT /evidence="ECO:0000250|UniProtKB:A0A109PTH9"
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"
SQ SEQUENCE 528 AA; 59616 MW; E3A47994771BCA32 CRC64;
MKLNLKASGV ARQLTTLAKT VAALSVLTAC ASSNTATVSS AMSKANGVFL ESQTKITNGA
LHFDGKKLNH NTFEKPSLGP EYDYFFGKNI SAHGDAVKPY KHYVFMTWYK GGKEQRNVML
SRFNTKTGVV KTIQFPHRHT GFRGNPLVGE SHNTIGLAVS PKNGTIHMVY DMHAYVDDDE
SGRFKGRFVD DFFRYSFSVP GAADVPDDEF TLEKFVKDTS EVSQGTDDFK HLTMTGNLED
KDNFSALTYP KFYKSKEGEL LHYMRWGGNN NGAYYFNKYD AEKQVWTRFT PFNHKDQETH
GNAYNWGLYG QMKYINGKLR VGFQQRSANN NDRYKYQNGV YYAYSDHPDG LGDWKNVDGE
NMTWPLVDSD EIKIFEPGDY IDHQEPNSVH IVGGFDWTVT ENEDLHFITH VRSTNTKRSD
YKEVSIHAFK PANAKDFTVT TDFTGADSIY TSGDSIFIIG LKNGYPFVEK AKGGTNEFEV
VYQQTSGVKF DHGTIHIENG KAYYYLMEKG AGNSLPLHLQ VIDLGVSR
