ID   ALGL_PSEPG              Reviewed;         367 AA.
AC   B0KGQ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=PputGB1_4568;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-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; CP000926; ABZ00455.1; -; Genomic_DNA.
DR   RefSeq; WP_012274107.1; NC_010322.1.
DR   AlphaFoldDB; B0KGQ9; -.
DR   SMR; B0KGQ9; -.
DR   STRING; 76869.PputGB1_4568; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   EnsemblBacteria; ABZ00455; ABZ00455; PputGB1_4568.
DR   KEGG; ppg:PputGB1_4568; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
DR   HOGENOM; CLU_064286_0_0_6; -.
DR   OMA; AAWSVMA; -.
DR   Proteomes; UP000002157; 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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           25..367
FT                   /note="Alginate lyase"
FT                   /id="PRO_5000304896"
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;  41143 MW;  883E8DE6BA7AE799 CRC64;
     MTLLKRISSP ALLALALFGG AAHAALVPPQ GYYEGIEKLK TGDGNFRCEA APKPYTGALQ
     FRSKYEGSDK ARATLNVASE KAFRKSTEDI TTLEKGVSKM VGQYMRDGRP AQLDCTLAWL
     GTWARADALL STDYNHTGKS MRKWALGSMS GSWLRLKFSH SQPLAAHQAE AEVIEKWFAR
     LAEQTVRDWS DLPLEKINNH SYWAAWSVMA TAVATDRRDL FDWAVKEYKV GANQVDDQGF
     LPNEIKRKQR ALAYHNYALP PLAMIASFAQ ANGVDLRKEN NFALQRLGEG VLAGARDPSQ
     FKARTGEKQD MKDLKVDSKY AWLEPWCELY HCVGDTLQRK HGMQPFNSFR LGGDLTRVYD
     PNAESKK