ID   ALGL_PSEPW              Reviewed;         367 AA.
AC   B1J479;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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};
GN   OrderedLocusNames=PputW619_0882;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA71387.1; -; Genomic_DNA.
DR   RefSeq; WP_012312810.1; NC_010501.1.
DR   AlphaFoldDB; B1J479; -.
DR   SMR; B1J479; -.
DR   STRING; 390235.PputW619_0882; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   EnsemblBacteria; ACA71387; ACA71387; PputW619_0882.
DR   KEGG; ppw:PputW619_0882; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
DR   HOGENOM; CLU_064286_0_0_6; -.
DR   OMA; AAWSVMA; -.
DR   OrthoDB; 804604at2; -.
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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           25..367
FT                   /note="Alginate lyase"
FT                   /id="PRO_5000314720"
FT   BINDING         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         136..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
SQ   SEQUENCE   367 AA;  41551 MW;  134DA37A99FF6665 CRC64;
     MTAFKRIFSP ALLVLALYGG AAHAALVPPQ GYYEGIEKIK TSDGNFRCES APKPFTGALQ
     FRSKYEGSDK ARATLNRDSE QAFRDSTKDI TTLERGVAKM VNQYMRDGRP AQLDCTLTWL
     GTWARADALM STNYNHTGKS MRKWALGSMS GSWLRLKFSN SQPLAAHQAE AELIEKWFAR
     LAEQTVRDWS NLPLEKINNH SYWAAWSVMA TAVATDRRDL FDWAVKEYKV GANQIDDQGF
     LPNEIKRKQR ALAYHNYALP PLAMIASFAK ANGVDLRSEN NFALQRLGEG VLYGARDPRH
     FAERAGEKQD MKDLKVDGKY AWLEPWCALY QCVGDTLERK HRMQPFDSFR LGGNLTRVYD
     PSAQSKK