ALYA_KLEPN
ID ALYA_KLEPN Reviewed; 307 AA.
AC Q59478;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Alginate lyase;
DE EC=4.2.2.3;
DE AltName: Full=Poly(beta-D-mannuronate) lyase;
DE AltName: Full=Poly(mana) alginate lyase;
DE Flags: Precursor;
GN Name=alyA;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-51.
RC STRAIN=Subsp. aerogenes 25;
RX PubMed=8200539; DOI=10.1016/0378-1119(94)90605-x;
RA Baron A.J., Wong T.Y., Hicks S.J., Gacesa P., Willcock D., McPherson M.J.;
RT "Alginate lyase from Klebsiella pneumoniae, subsp. aerogenes: gene cloning,
RT sequence analysis and high-level production in Escherichia coli.";
RL Gene 143:61-66(1994).
CC -!- FUNCTION: Degrades alginates that contain guluronic acid.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 7 family.
CC {ECO:0000305}.
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DR EMBL; L19657; AAA25049.1; -; Genomic_DNA.
DR PDB; 4OZX; X-ray; 1.88 A; A=23-307.
DR PDBsum; 4OZX; -.
DR AlphaFoldDB; Q59478; -.
DR SMR; Q59478; -.
DR CAZy; PL7; Polysaccharide Lyase Family 7.
DR BRENDA; 4.2.2.3; 2814.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045135; F:poly(beta-D-mannuronate) lyase activity; IEA:UniProtKB-EC.
DR InterPro; IPR014895; Alginate_lyase_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR Pfam; PF08787; Alginate_lyase2; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8200539"
FT CHAIN 21..307
FT /note="Alginate lyase"
FT /id="PRO_0000024925"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4OZX"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:4OZX"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4OZX"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4OZX"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 130..145
FT /evidence="ECO:0007829|PDB:4OZX"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4OZX"
FT STRAND 291..302
FT /evidence="ECO:0007829|PDB:4OZX"
SQ SEQUENCE 307 AA; 33512 MW; 76A1F9AAE082632E CRC64;
MLKSGVMVAS LCLFSVPSRA AVPAPGDKFE LSGWSLSVPV DSDNDGKADQ IKEKTLAAGY
RNSDFFTLSD AGGMVFKAPI SGAKTSKNTT YTRSELREML RKGDTSIATQ GVSRNNWVLS
SAPLSEQKKA GGVDGTLEAT LSVDHVTTTG VNWQVGRVII GQIHANNDEP IRLYYRKLPH
HQKGSVYFAH EPRKGFGDEQ WYEMIGTLQP SHGNQTAAPT EPEAGIALGE TFSYRIDATG
NKLTVTLMRE GRPDVVKTVD MSKSGYSEAG QYLYFKAGVY NQNKTGKPDD YVQATFYRLK
ATHGAQR