ID   ALGL_COBMA              Reviewed;         374 AA.
AC   Q9ZNB7;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; Synonyms=alg;
OS   Cobetia marina (Deleya marina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Cobetia.
OX   NCBI_TaxID=28258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N-1;
RA   Kraiwattanapong J., Ooi T., Kinoshita S.;
RT   "Alginate lyase gene from Deleya marina.";
RL   Submitted (OCT-1998) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB018795; BAA33966.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZNB7; -.
DR   SMR; Q9ZNB7; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   BRENDA; 4.2.2.3; 5136.
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..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           27..374
FT                   /note="Alginate lyase"
FT                   /id="PRO_0000024917"
FT   BINDING         67..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         140..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
SQ   SEQUENCE   374 AA;  42219 MW;  416616B1D8A2E0FA CRC64;
     MRNPKLKNLL APTLLSLAMF AGATQAAAPL RPPQGYFAPV DKFKTGDKSD GCDAMPAPYT
     GPLQFRSKYE GSDKARATLN VQSEKAFRDT TKDITTLERG TAKRVMQFMR DGRPEQLECT
     LNWLTAWAKA DALMSKDFNH TGKSMRKWAL GSMASSYIRL KFSDSHPLAQ HQQEAQLIEA
     WFSKMADQVV SDWDNLPLEK TNNHSYWAAW SVMATAVATN RRDLFDWAVK EYKVGVNQVD
     ADGFLPNELK RQQRALAYHN YALPPLAMIA SFAQINGVDL RQENNGALKR LGDRVLAGVK
     DPDEFEEKNG KKQDMTDLKE DMKFAWLEPF CTLYTCAPDV IEKKRDMQPF KTFRLGGDLT
     KVYDPSHEKG NKGS