ID   ALGL_AZOCH     STANDARD;      PRT;   372 AA.
AC   O50660;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-MAY-2006, entry version 32.
DE   Alginate lyase precursor (EC 4.2.2.3) (Poly(beta-D-mannuronate) lyase)
DE   (Poly(mana) alginate lyase).
GN   Name=algL;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4412 / NCIB 8003 / X-50;
RX   MEDLINE=99175437; PubMed=10049370;
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: Depolymerizes alginate by cleaving the beta-1,4
CC       glycosidic bond. Degrades deacetylated polymannuronate alginate
CC       more efficiently than non-deacetylated polyM. Is able to degrade
CC       its own alginate, but at a lower efficiency than that produced
CC       from M.pyriferia and P.aeruginosa.
CC   -!- CATALYTIC ACTIVITY: Eliminative cleavage of polysaccharides
CC       containing beta-D-mannuronate residues to give oligosaccharides
CC       with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at
CC       their ends.
CC   -!- ENZYME REGULATION: Monovalent cations such as potassium and sodium
CC       enhance activity, as well as a combined action of these cations
CC       with magnesium. However, other cations like calcium, cobalt,
CC       manganese and zinc, or the presence of EDTA, do not affect the
CC       enzymatic activity.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
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DR   EMBL; AJ223605; CAA11481.1; -; Genomic_DNA.
DR   HAMAP; MF_00557; -; 1.
DR   InterPro; IPR008397; Alginate_lyase.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   Pfam; PF05426; Alginate_lyase; 1.
KW   Lyase; Periplasmic; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    372       Alginate lyase.
FT                                /FTId=PRO_0000024915.
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
//