ID   ALGL_PSEFL              Reviewed;         373 AA.
AC   P59786;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17397 / DSM 50091 / CIP 73.25 / NCIMB 10525 / 12;
RX   PubMed=12775688; DOI=10.1128/jb.185.12.3515-3523.2003;
RA   Gimmestad M., Sletta H., Ertesvaag H., Bakkevig K., Jain S., Suh S.-J.,
RA   Skjaak-Braek G., Ellingsen T.E., Ohman D.E., Valla S.;
RT   "The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-
RT   epimerase activity, is needed for alginate polymer formation.";
RL   J. Bacteriol. 185:3515-3523(2003).
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; AF527790; AAP46696.1; -; Genomic_DNA.
DR   RefSeq; WP_012722329.1; NZ_LACG01000011.1.
DR   AlphaFoldDB; P59786; -.
DR   SMR; P59786; -.
DR   STRING; 690597.JH730920_gene1194; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   PATRIC; fig|294.129.peg.5007; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
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..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           26..373
FT                   /note="Alginate lyase"
FT                   /id="PRO_0000024919"
FT   BINDING         66..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         139..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
SQ   SEQUENCE   373 AA;  42323 MW;  77A9C242BD9A8181 CRC64;
     MRLPMQKLLI PTLLGLAMFA GSVNAAAPLR PPQGYFAPVE AFKTGDFKND CDAMPPPYTG
     SLQFRSKYEG SDKARSTLNV QSEKAFRDST ADITKLEKDT SKRVMQFMRD GRPEQLECTL
     NWLTSWAKAD ALMSKDFNHT GKSMRKWALG SMASAYVRLK FSDSHPLANH QQESQLIEAW
     FNKLADQVVS DWDNLPLEKT NNHSYWAAWS VMATSVATNR RDLFDWAVKE YKVGVNQVDD
     QGFLPNELKR QQRALSYHNY ALPPLSMIAS FALVNGVDLR QENNSALKRL GDKVLAGVKD
     PEIFEKKNGK EQDMKDLKED MKYAWLEPFC TLYTCAPDVI ERKHGMQPFK TFRLGGDLTK
     VYDPTHEKGN KGS