ID   ALGL_AZOCH              Reviewed;         372 AA.
AC   O50660;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Alginate lyase {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000303|PubMed:10049370};
DE            EC=4.2.2.3 {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:10049370};
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, ECO:0000303|PubMed:10049370};
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 4412 / NCIMB 8003 / NRS 7 / X-50;
RX   PubMed=10049370; DOI=10.1128/jb.181.5.1409-1414.1999;
RA   Pecina A., Pascual A., Paneque A.;
RT   "Cloning and expression of the algL gene, encoding the Azotobacter
RT   chroococcum alginate lyase: purification and characterization of the
RT   enzyme.";
RL   J. Bacteriol. 181:1409-1414(1999).
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       alginate more efficiently than non-deacetylated polyM. Is able to
CC       degrade its own alginate, but at a lower efficiency than that produced
CC       from M.pyriferia and P.aeruginosa (PubMed:10049370). May serve to
CC       degrade mislocalized alginate that is trapped in the periplasmic space
CC       (By similarity). {ECO:0000255|HAMAP-Rule:MF_00557,
CC       ECO:0000269|PubMed:10049370}.
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:10049370};
CC   -!- ACTIVITY REGULATION: Monovalent cations such as potassium and sodium
CC       enhance activity, as well as a combined action of these cations with
CC       magnesium. However, other cations like calcium, cobalt, manganese and
CC       zinc, or the presence of EDTA, do not affect the enzymatic activity.
CC       {ECO:0000269|PubMed:10049370}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:10049370};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:10049370};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10049370}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00557}.
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DR   EMBL; AJ223605; CAA11481.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50660; -.
DR   SMR; O50660; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   BRENDA; 4.2.2.3; 617.
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   Lyase; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           23..372
FT                   /note="Alginate lyase"
FT                   /id="PRO_0000024915"
FT   BINDING         61..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         134..135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
SQ   SEQUENCE   372 AA;  41321 MW;  23F6D24181038B18 CRC64;
     MKTRLALPCL LGSLLLSSAV HAASALVPPK GYYAALEIRK GEAQACQAVP EPYTGELVFR
     SKYEGSDSAR STLNKKAEKA FRAKTKPITE IERGVSRMVM RYMEKGRLRR AGMRPGLLDA
     WAEDDALLST EYNHTGKSMR KWALGSLAGA YLRLKFSTSQ PLAAYPEQAK RIEAWFAKVG
     DQVIKDWSDL PLKQINNHSY WAAWSVMAAG VATNRRPLFD WAVEQFHIAA KQVDPRGFLA
     NELKRRQRAL AYHNYSLPPL MMIAAFAQAN GVDLRGDNDG ALGRLAGNVL AGVEDPEPFA
     ERAGEDQDME DLETDAKFSW LEPYCALYAC SPALRERKAE MGPFKNFRLG GDVTRIFDPQ
     EKPSKSTVGN AD