ID   ALGL_PSESY              Reviewed;         378 AA.
AC   Q9L7P2;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Alginate lyase {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000303|PubMed:11029455};
DE            EC=4.2.2.3 {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:11029455};
DE   AltName: Full=Poly(beta-D-mannuronate) lyase {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000305|PubMed:11029455};
DE   Flags: Precursor;
GN   Name=algL {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000303|PubMed:11029455};
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-38, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   HIS-204 AND TRP-207.
RC   STRAIN=FF5;
RX   PubMed=11029455; DOI=10.1128/jb.182.21.6268-6271.2000;
RA   Preston L.A., Wong T.Y., Bender C.L., Schiller N.L.;
RT   "Characterization of alginate lyase from Pseudomonas syringae pv.
RT   syringae.";
RL   J. Bacteriol. 182:6268-6271(2000).
CC   -!- FUNCTION: Catalyzes the depolymerization of alginate by cleaving the
CC       beta-1,4 glycosidic bond between two adjacent sugar residues via a
CC       beta-elimination mechanism. Degrades deacetylated polymannuronate
CC       (polyM) alginate from P.aeruginosa more efficiently than non-
CC       deacetylated polyM and alginate from M.pyrifera. AlgL from P.syringae
CC       degrades also its own alginate, which may indicate a role in cleaving
CC       preformed alginate and/or in determining the length of the alginate
CC       polymer (PubMed:11029455). May serve to degrade mislocalized alginate
CC       that is trapped in the periplasmic space (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:11029455}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of alginate to give oligosaccharides with
CC         4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing
CC         ends and beta-D-mannuronate at their reducing end.; EC=4.2.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00557,
CC         ECO:0000269|PubMed:11029455};
CC   -!- ACTIVITY REGULATION: The monovalent cation sodium enhances activity but
CC       is not absolutely required. {ECO:0000269|PubMed:11029455}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:11029455};
CC       Temperature dependence:
CC         Optimum temperature is 42 degrees Celsius.
CC         {ECO:0000269|PubMed:11029455};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11029455}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00557}.
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; AF222020; AAF32371.1; -; Genomic_DNA.
DR   RefSeq; WP_003365409.1; NZ_MLEV01000001.1.
DR   AlphaFoldDB; Q9L7P2; -.
DR   SMR; Q9L7P2; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   PATRIC; fig|321.63.peg.1597; -.
DR   BRENDA; 4.2.2.3; 5193.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045135; F:poly(beta-D-mannuronate) lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042122; P:alginic acid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00244; AlgLyase; 1.
DR   Gene3D; 1.50.10.100; -; 1.
DR   HAMAP; MF_00557; Alginate_lyase; 1.
DR   InterPro; IPR022859; Alginate_lyase.
DR   InterPro; IPR008397; Alginate_lyase_dom.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   Pfam; PF05426; Alginate_lyase; 1.
DR   SUPFAM; SSF48230; SSF48230; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Periplasm; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:11029455"
FT   CHAIN           29..378
FT                   /note="Alginate lyase"
FT                   /id="PRO_0000024922"
FT   BINDING         67..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         140..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   MUTAGEN         204
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11029455"
FT   MUTAGEN         207
FT                   /note="W->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11029455"
SQ   SEQUENCE   378 AA;  42542 MW;  33E5894BC6404F14 CRC64;
     MQTPKLIRPT LLSMAILSSM AWATGASAAL VPPKGYDAPI EKMKTGDHNF SCEAIPKPYT
     DKLVFRSKYE GSDKARATLN AVSEEAFRDA TKDITTLERG VSKVVMQYMR DGRPEQLDCA
     LNMMTTWAKA DALESREFNH TGKSMRKWAL GSMSSAYLRL KFSESHPLAN RQQDAKIIET
     WFSKLADQVV SDWSNLPLEK INNHSYWAAW SVMATAVATN RQDLFDWAVK EYKVAANQVD
     KDGFLPNEMK RRQRALSYHN YALPPLAMIA SFAQANGVDL RPENNGALKR LGDRVLAGVK
     DPSIFAEHNG EKQDMTDLKK DPKFAWLEPY CSLYTCSPDV LEEKHEKQPF KTFRLGGDLT
     KVYDPTHEKG DKGDNDGS