ID   ALGL_PSEPF              Reviewed;         374 AA.
AC   Q3KHR0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alginate lyase {ECO:0000255|HAMAP-Rule:MF_00557};
DE            EC=4.2.2.3 {ECO:0000255|HAMAP-Rule:MF_00557};
DE   AltName: Full=Poly(beta-D-mannuronate) lyase {ECO:0000255|HAMAP-Rule:MF_00557};
DE   Flags: Precursor;
GN   Name=algL {ECO:0000255|HAMAP-Rule:MF_00557}; OrderedLocusNames=Pfl01_0953;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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. May serve to degrade mislocalized alginate
CC       that is trapped in the periplasmic space. {ECO:0000255|HAMAP-
CC       Rule:MF_00557}.
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00557}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00557}.
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DR   EMBL; CP000094; ABA72696.1; -; Genomic_DNA.
DR   RefSeq; WP_011332553.1; NC_007492.2.
DR   AlphaFoldDB; Q3KHR0; -.
DR   SMR; Q3KHR0; -.
DR   STRING; 205922.Pfl01_0953; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   EnsemblBacteria; ABA72696; ABA72696; Pfl01_0953.
DR   KEGG; pfo:Pfl01_0953; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
DR   HOGENOM; CLU_064286_0_0_6; -.
DR   OMA; AAWSVMA; -.
DR   Proteomes; UP000002704; Chromosome.
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   3: Inferred from homology;
KW   Lyase; Periplasm; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           27..374
FT                   /note="Alginate lyase"
FT                   /id="PRO_5000001586"
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"
SQ   SEQUENCE   374 AA;  42113 MW;  D133F033DC12D47C CRC64;
     MRNPKLKTLL APTLLGLAIF AGTAQAAAPL RPPQGYFAPV DKFKTGDKSE GCDAMPTPYT
     GPLQFRSKYE GSDKARATLN VQSEKAFRDT TKDITTLERG TAKRVMQFMR DGRPEQLDCT
     LNWLTAWAKA DALMSKDFNH TGKSMRKWAL GSMASSYIRL KFSDSHPLAQ HQQEAQVIEA
     WFSKMADQVV SDWDNLPLEK TNNHSYWAAW SVMATSVATN RRDLFDWAVK EYKVGVNQVD
     ADGFLPNELK RQQRALAYHN YALPPLAMIA SFAQVNGVDL RQENNGALKR LGDRVLAGVK
     DPDQFEKKNG KEQDMTDLKQ DMKFAWLEPF CTLYTCSPDV IEKKHGMQPF KTFRLGGDLT
     KVYDPSHEKG NKGS