ALGL_PSEAE
ID ALGL_PSEAE Reviewed; 367 AA.
AC Q06749; Q57292;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Alginate lyase {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000303|PubMed:8335634, ECO:0000303|PubMed:8370530};
DE EC=4.2.2.3 {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:23215237};
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:8335634,
GN ECO:0000303|PubMed:8370530}; OrderedLocusNames=PA3547;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=8830;
RX PubMed=8370530; DOI=10.1016/0378-1119(93)90662-m;
RA Boyd A., Ghosh M., May T.B., Shinabarger D., Keogh R., Chakrabarty A.M.;
RT "Sequence of the algL gene of Pseudomonas aeruginosa and purification of
RT its alginate lyase product.";
RL Gene 131:1-8(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-43, FUNCTION,
RP INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=FRD1;
RX PubMed=8335634; DOI=10.1128/jb.175.15.4780-4789.1993;
RA Schiller N.L., Monday S.R., Boyd C.M., Keen N.T., Ohman D.E.;
RT "Characterization of the Pseudomonas aeruginosa alginate lyase gene (algL):
RT cloning, sequencing, and expression in Escherichia coli.";
RL J. Bacteriol. 175:4780-4789(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FRD1;
RX PubMed=16177314; DOI=10.1128/iai.73.10.6429-6436.2005;
RA Jain S., Ohman D.E.;
RT "Role of an alginate lyase for alginate transport in mucoid Pseudomonas
RT aeruginosa.";
RL Infect. Immun. 73:6429-6436(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23215237; DOI=10.1021/bi301425r;
RA Farrell E.K., Tipton P.A.;
RT "Functional characterization of AlgL, an alginate lyase from Pseudomonas
RT aeruginosa.";
RL Biochemistry 51:10259-10266(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 28-362 OF WILD-TYPE AND MUTANT
RP ALA-202 IN COMPLEX WITH BETA-D-MANNURONATE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Howell P.L., Wolfram F., Robinson H., Arora K.;
RT "Crystal structure of the periplasmic alginate lyase AlgL and the AlgL
RT H202A mutant.";
RL Submitted (FEB-2014) to the PDB data bank.
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 (PubMed:8370530, PubMed:8335634,
CC PubMed:23215237). May serve to degrade mislocalized alginate that is
CC trapped in the periplasmic space. Acts preferentially on non-acetylated
CC alginate or its precursor mannuronan. Is able to catalyze cleavage
CC adjacent to either mannuronate or guluronate residues in alginate.
CC Exhaustive digestion of alginate by AlgL generates dimeric and trimeric
CC products (PubMed:23215237). In addition to its enzymatic function, AlgL
CC appears to be required for alginate export, maybe as part of a multi-
CC protein alginate-secretion complex (PubMed:16177314).
CC {ECO:0000269|PubMed:16177314, ECO:0000269|PubMed:23215237,
CC ECO:0000269|PubMed:8335634, ECO:0000269|PubMed:8370530}.
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:23215237};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for mannuronan (dp value of 133)
CC {ECO:0000269|PubMed:23215237};
CC KM=5 uM for acetylated mannuronan (dp value of 133)
CC {ECO:0000269|PubMed:23215237};
CC KM=13 uM for alginate (dp value of 263)
CC {ECO:0000269|PubMed:23215237};
CC KM=2.6 uM for acetylated alginate (dp value of 263)
CC {ECO:0000269|PubMed:23215237};
CC Note=kcat is 32 sec(-1) for the depolymerization of mannuronan (dp
CC value of 133). kcat is 1.5 sec(-1) for the depolymerization of
CC acetylated mannuronan (dp value of 133). kcat is 32 sec(-1) for the
CC depolymerization of alginate (dp value of 263). kcat is 1.2 sec(-1)
CC for the depolymerization of acetylated alginate (dp value of 263).
CC The catalytic efficiency of the depolymerization reaction increases
CC linearly with the number of residues in the substrate.
CC {ECO:0000269|PubMed:23215237};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00557,
CC ECO:0000269|PubMed:8370530, ECO:0000305|PubMed:8335634}.
CC -!- INDUCTION: Its expression is under the control of AlgB, which also
CC regulates the alginate biosynthetic gene cluster.
CC {ECO:0000269|PubMed:8335634}.
CC -!- DISRUPTION PHENOTYPE: Deletion of algL is lethal, and microscopic
CC examination of the cells reveals that alginate or a precursor
CC accumulates in the periplasmic space until the cells burst.
CC {ECO:0000269|PubMed:16177314}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
CC {ECO:0000255|HAMAP-Rule:MF_00557}.
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DR EMBL; L14597; AAA71990.1; -; Unassigned_DNA.
DR EMBL; U27829; AAA91127.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06935.1; -; Genomic_DNA.
DR PIR; H83202; H83202.
DR PIR; JN0777; JN0777.
DR RefSeq; NP_252237.1; NC_002516.2.
DR RefSeq; WP_003092108.1; NZ_QZGE01000001.1.
DR PDB; 4OZV; X-ray; 1.64 A; A=28-362.
DR PDB; 4OZW; X-ray; 1.64 A; A=28-362.
DR PDBsum; 4OZV; -.
DR PDBsum; 4OZW; -.
DR AlphaFoldDB; Q06749; -.
DR SMR; Q06749; -.
DR STRING; 287.DR97_4395; -.
DR CAZy; PL5; Polysaccharide Lyase Family 5.
DR PaxDb; Q06749; -.
DR EnsemblBacteria; AAG06935; AAG06935; PA3547.
DR GeneID; 878552; -.
DR KEGG; pae:PA3547; -.
DR PATRIC; fig|208964.12.peg.3711; -.
DR PseudoCAP; PA3547; -.
DR HOGENOM; CLU_064286_0_0_6; -.
DR InParanoid; Q06749; -.
DR OMA; AAWSVMA; -.
DR PhylomeDB; Q06749; -.
DR BioCyc; PAER208964:G1FZ6-3615-MON; -.
DR BRENDA; 4.2.2.3; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:PseudoCAP.
DR GO; GO:0045135; F:poly(beta-D-mannuronate) lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0042122; P:alginic acid catabolic process; IDA:PseudoCAP.
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 3D-structure; Direct protein sequencing; Lyase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8335634"
FT CHAIN 28..367
FT /note="Alginate lyase"
FT /id="PRO_0000024918"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:4OZV"
FT BINDING 138..139
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:4OZV"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.6, ECO:0007744|PDB:4OZV"
FT CONFLICT 269
FT /note="A -> P (in Ref. 1; AAA71990)"
FT /evidence="ECO:0000305"
FT CONFLICT 337..341
FT /note="KMLEA -> NACSRP (in Ref. 1; AAA71990)"
FT /evidence="ECO:0000305"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4OZW"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 90..109
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:4OZW"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 138..160
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 170..191
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 220..236
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 253..273
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4OZW"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4OZW"
SQ SEQUENCE 367 AA; 40829 MW; EAA3FE30032AB3BA CRC64;
MKTSHLIRIA LPGALAAALL ASQVSQAADL VPPPGYYAAV GERKGSAGSC PAVPPPYTGS
LVFTSKYEGS DSARATLNVK AEKTFRSQIK DITDMERGAT KLVTQYMRSG RDGDLACALN
WMSAWARAGA LQSDDFNHTG KSMRKWALGS LSGAYMRLKF SSSRPLAAHA EQSREIEDWF
ARLGTQVVRD WSGLPLKKIN NHSYWAAWSV MSTAVVTNRR DLFDWAVSEF KVAANQVDEQ
GFLPNELKRR QRALAYHNYA LPPLAMIAAF AQVNGVDLRQ ENHGALQRLA ERVMKGVDDE
ETFEEKTGED QDMTDLKVDN KYAWLEPYCA LYRCEPKMLE AKKDREPFNS FRLGGEVTRV
FSREGGS
