ALGL_PSEFS
ID ALGL_PSEFS Reviewed; 373 AA.
AC C3KDZ3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PFLU_0983;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY47248.1; -; Genomic_DNA.
DR AlphaFoldDB; C3KDZ3; -.
DR SMR; C3KDZ3; -.
DR STRING; 216595.PFLU_0983; -.
DR CAZy; PL5; Polysaccharide Lyase Family 5.
DR PRIDE; C3KDZ3; -.
DR EnsemblBacteria; CAY47248; CAY47248; PFLU_0983.
DR KEGG; pfs:PFLU_0983; -.
DR eggNOG; ENOG502ZAMJ; Bacteria.
DR HOGENOM; CLU_064286_0_0_6; -.
DR OMA; AAWSVMA; -.
DR Proteomes; UP000002332; 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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT CHAIN 26..373
FT /note="Alginate lyase"
FT /id="PRO_5000460114"
FT BINDING 66..67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT BINDING 139..140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
SQ SEQUENCE 373 AA; 42323 MW; 77A9C242BD9A8181 CRC64;
MRLPMQKLLI PTLLGLAMFA GSVNAAAPLR PPQGYFAPVE AFKTGDFKND CDAMPPPYTG
SLQFRSKYEG SDKARSTLNV QSEKAFRDST ADITKLEKDT SKRVMQFMRD GRPEQLECTL
NWLTSWAKAD ALMSKDFNHT GKSMRKWALG SMASAYVRLK FSDSHPLANH QQESQLIEAW
FNKLADQVVS DWDNLPLEKT NNHSYWAAWS VMATSVATNR RDLFDWAVKE YKVGVNQVDD
QGFLPNELKR QQRALSYHNY ALPPLSMIAS FALVNGVDLR QENNSALKRL GDKVLAGVKD
PEIFEKKNGK EQDMKDLKED MKYAWLEPFC TLYTCAPDVI ERKHGMQPFK TFRLGGDLTK
VYDPTHEKGN KGS