ID   ALGL_AZOVI              Reviewed;         374 AA.
AC   O52195;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Alginate lyase {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000303|PubMed:9683471};
DE            EC=4.2.2.3 {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:9683471};
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:9683471};
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=E;
RX   PubMed=9683471; DOI=10.1128/jb.180.15.3779-3784.1998;
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: 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. Splits ManA-ManA and ManA-GulA bonds, but
CC       not GulA-ManA or GulA-GulA bonds. Also cleaves acetylated residues
CC       (PubMed:9683471). May serve to degrade mislocalized alginate that is
CC       trapped in the periplasmic space (By similarity). {ECO:0000255|HAMAP-
CC       Rule:MF_00557, ECO:0000269|PubMed:9683471}.
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:9683471};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.1-8.4. {ECO:0000269|PubMed:9683471};
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; AF027499; AAC04567.1; -; Genomic_DNA.
DR   EMBL; AF037600; AAC32313.1; -; Genomic_DNA.
DR   RefSeq; WP_012699742.1; NZ_FPKM01000036.1.
DR   AlphaFoldDB; O52195; -.
DR   SMR; O52195; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   BRENDA; 4.2.2.3; 49.
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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           24..374
FT                   /note="Alginate lyase"
FT                   /id="PRO_0000024916"
FT   BINDING         62..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         135..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
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