ID   ALGL_PSEU2              Reviewed;         378 AA.
AC   Q4ZXL0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, 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=Psyr_1056;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY36112.1; -; Genomic_DNA.
DR   RefSeq; WP_004406765.1; NC_007005.1.
DR   RefSeq; YP_234150.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZXL0; -.
DR   SMR; Q4ZXL0; -.
DR   STRING; 205918.Psyr_1056; -.
DR   CAZy; PL5; Polysaccharide Lyase Family 5.
DR   EnsemblBacteria; AAY36112; AAY36112; Psyr_1056.
DR   KEGG; psb:Psyr_1056; -.
DR   PATRIC; fig|205918.7.peg.1086; -.
DR   eggNOG; ENOG502ZAMJ; Bacteria.
DR   HOGENOM; CLU_064286_0_0_6; -.
DR   OMA; AAWSVMA; -.
DR   Proteomes; UP000000426; 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; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00557"
FT   CHAIN           29..378
FT                   /note="Alginate lyase"
FT                   /id="PRO_5000000624"
FT   REGION          359..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   378 AA;  42439 MW;  9E7F9120396267F2 CRC64;
     MQTPKLIRPT LLSMAILSSM AWATGASAAL VPPKGYDAPI EKIKTGDHSF SCEAIPKPYT
     DKLVFRSKYE GSDKARATLN AVSEEAFRDA TKDITTLERG VSKVVMQYMR DGRPEQLDCA
     LNMMTTWAKA DALESREFNH TGKSMRKWAL GSMSSAYLRL KFSESHPLAN RQQDAKIIEA
     WFSKLADQVV SDWSNLPLDK INNHSYWAAW SVMATAVATN RQDLFDWAVK EYKVAANQVD
     KDGFLPNEMK RRQRALSYHN YALPPLAMIA SFAQANGVDL RPENNGALKR LGDRVLAGVK
     DPSIFAEHNG EKQDMTDLKK DPKFAWLEPY CSLYTCSPDV LEEKHEKQPF KTFRLGGDLT
     KVYDPSHEKG DKGDNDGS