ID   ALGL_AZOVI     STANDARD;      PRT;   374 AA.
AC   O52195;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Alginate lyase precursor (EC 4.2.2.3) (Poly(beta-D-mannuronate) lyase)
DE   (Poly(mana) alginate lyase).
GN   Name=algL;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 9046;
RA   Vazquez R.A., Alvarado D.A., Guzman J., Soberon-Chavez G., Espin G.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E;
RX   MEDLINE=98348436; PubMed=9683471;
RA   Ertesvag H., Erlien F., Skjak-Braek G., Rehm B.H., Valla S.;
RT   "Biochemical properties and substrate specificities of a recombinantly
RT   produced Azotobacter vinelandii alginate lyase.";
RL   J. Bacteriol. 180:3779-3784(1998).
CC   -!- FUNCTION: Depolymerizes alginate by cleaving the beta-1,4
CC       glycosidic bond. Splits ManA-ManA and ManA-GulA bonds, but not
CC       GulA-ManA or GulA-GulA bonds. Also cleaves acetylated residues.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.1-8.4;
CC   -!- SUBCELLULAR LOCATION: Periplasmic (By similarity).
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF027499; AAC04567.1; -.
DR   EMBL; AF037600; AAC32313.1; -.
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     23       Potential.
FT   CHAIN        24    374       Alginate lyase.
SQ   SEQUENCE   374 AA;  41404 MW;  89FAF1CC0CA74961 CRC64;
     MHKTRLALSC LLGSLLLSGA VHAAEALVPP KGYYAPVDIR KGEAPACPVV PEPFTGELVF
     RSKYEGSDAA RSTLNEEAEK AFRTKTAPIT QIERGVSRMV MRYMEKGRAG DLECTLAWLD
     AWAEDGALLT TEYNHTGKSM RKWALGSLAG AYLRLKFSSS QPLAAYPEQA RRIESWFAKV
     GDQVIKDWSD LPLKRINNHS YWAAWAVMAA GVATNRRPLF DWAVEQFHIA AGQVDSNGFL
     PNELKRRQRA LAYHNYSLPP LMMVAAFALA NGVDLRGDND GALGRLAGNV LAGVEKPEPF
     AERAGDEDQD MEDLETDAKF SWLEPYCALY SCSPALRERK AEMGPFKNFR LGGDVTRIFD
     PAEKSPRSTV GKRD
//