Reviewed, UniProtKB/Swiss-Prot O52195 (ALGL_AZOVI)

Names and origin

Protein names

Recommended name:
    Alginate lyase
    EC=4.2.2.3
Alternative name(s):
    Poly(beta-D-mannuronate) lyase
    Poly(mana) alginate lyase

Gene names

Name:

algL

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Depolymerizes alginate by cleaving the beta-1,4 glycosidic bond. Splits ManA-ManA and ManA-GulA bonds, but not GulA-ManA or GulA-GulA bonds. Also cleaves acetylated residues. HAMAP MF_00557
Catalytic activity	Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. HAMAP MF_00557
Subcellular location	Periplasm By similarity HAMAP MF_00557.
Sequence similarities	Belongs to the polysaccharide lyase 5 family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.1-8.4. HAMAP MF_00557

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Lyase
Gene Ontology (GO)
Biological process	alginic acid catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	poly(beta-D-mannuronate) lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 374	351	Alginate lyase HAMAP MF_00557		PRO_0000024916

Sequences

	Sequence		Length	Mass (Da)
	O52195-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 89FAF1CC0CA74961	FASTA	374	41,404
	10 20 30 40 50 60 MHKTRLALSC LLGSLLLSGA VHAAEALVPP KGYYAPVDIR KGEAPACPVV PEPFTGELVF 70 80 90 100 110 120 RSKYEGSDAA RSTLNEEAEK AFRTKTAPIT QIERGVSRMV MRYMEKGRAG DLECTLAWLD 130 140 150 160 170 180 AWAEDGALLT TEYNHTGKSM RKWALGSLAG AYLRLKFSSS QPLAAYPEQA RRIESWFAKV 190 200 210 220 230 240 GDQVIKDWSD LPLKRINNHS YWAAWAVMAA GVATNRRPLF DWAVEQFHIA AGQVDSNGFL 250 260 270 280 290 300 PNELKRRQRA LAYHNYSLPP LMMVAAFALA NGVDLRGDND GALGRLAGNV LAGVEKPEPF 310 320 330 340 350 360 AERAGDEDQD MEDLETDAKF SWLEPYCALY SCSPALRERK AEMGPFKNFR LGGDVTRIFD 370 PAEKSPRSTV GKRD

References

[1]	Vazquez R.A., Alvarado D.A., Guzman J., Soberon-Chavez G., Espin G. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 9046.
[2]	"Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase." Ertesvag H., Erlien F., Skjak-Braek G., Rehm B.H., Valla S. J. Bacteriol. 180:3779-3784(1998) [PubMed: 9683471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF027499 Genomic DNA. Translation: AAC04567.1. AF037600 Genomic DNA. Translation: AAC32313.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	PL5. Polysaccharide Lyase Family 5.
Enzyme and pathway databases
BRENDA	4.2.2.3. 883.
Family and domain databases
HAMAP	MF_00557. Alginate_lyase. [Tree]
InterPro	IPR008397. Alginate_lyase. IPR008929. Chondroitin_lyas. [Graphical view]
Gene3D	G3DSA:1.50.10.110. Alginate_lyase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALGL_AZOVI

Accession

Primary (citable) accession number: O52195

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)