ID   ALGL_PSEF5              Reviewed;         371 AA.
AC   Q4KHY5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=PFL_1017;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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}.
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DR   EMBL; CP000076; AAY90304.1; -; Genomic_DNA.
DR   RefSeq; WP_011059370.1; NC_004129.6.
DR   AlphaFoldDB; Q4KHY5; -.
DR   SMR; Q4KHY5; -.
DR   STRING; 220664.PFL_1017; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   EnsemblBacteria; AAY90304; AAY90304; PFL_1017.
DR   GeneID; 57474022; -.
DR   KEGG; pfl:PFL_1017; -.
DR   PATRIC; fig|220664.5.peg.1043; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
DR   HOGENOM; CLU_064286_0_0_6; -.
DR   OMA; AAWSVMA; -.
DR   OrthoDB; 804604at2; -.
DR   Proteomes; UP000008540; Chromosome.
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; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           27..371
FT                   /note="Alginate lyase"
FT                   /id="PRO_1000061112"
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   371 AA;  41682 MW;  C2E09D7BCB8BB119 CRC64;
     MQSTDLKRLL IPSLLGLAIV TGSAQAAAPL RPPQGYYAPV DKFKSGDNSE GCDAMPAPYT
     GALQFRSKYE GSDKARATLN VQSEQAFRDT TADITKIERG TSKRVMQFMR DGRPEQLDCT
     LAWLSAWAQA DALMSKDFNH TGKSMRKWAL GSMASAYLRL KFSDSHPLAT HQEQAQKIEA
     WFSKMADQVV SDWDNLPLDK TNNHSYWAAW SVMATAVATN RRDLFDWAVK EYKVGANQVD
     ADGFLPNELK RQQRALAYHN YALPPLAMIA SFAQVNGVDL RQENHEALKR LGERVLAGVK
     DPDTFEKKNG KQQDMTDLKV DSKFAWLEPY CSLYTCAPET LERKHKMQPF KTFRLGGDLT
     KVYDPAHEKG S